Signaling proteins that are ligands for the EPH FAMILY RECEPTORS. They are membrane-bound proteins that are attached to the CELL MEMBRANE either through a GLYCOINOSITOL PHOSPHOLIPID MEMBRANE ANCHOR or through a transmembrane domain. Many of the ephrins are considered important intercellular signaling molecules that control morphogenic changes during embryogenesis.
A large family of receptor protein-tyrosine kinases that are structurally-related. The name of this family of proteins derives from original protein Eph (now called the EPHA1 RECEPTOR), which was named after the cell line it was first discovered in: Erythropoietin-Producing human Hepatocellular carcinoma cell line. Members of this family have been implicated in regulation of cell-cell interactions involved in nervous system patterning and development.
A transmembrane domain containing ephrin that binds with high affinity to EPHB1 RECEPTOR; EPHB3 RECEPTOR; and EPHB4 RECEPTOR. Expression of ephrin-B2 occurs in a variety of adult tissues. During embryogenesis, high levels of ephrin-B2 is seen in the PROSENCEPHALON; RHOMBENCEPHALON; developing SOMITES; LIMB BUD; and bronchial arches.
A transmembrane domain containing ephrin that is specific for EPHB1 RECEPTOR; EPHB2 RECEPTOR and EPHB3 RECEPTOR. It is widely expressed in a variety of developing and adult tissues.
A GLYCOINOSITOL PHOSPHOLIPID MEMBRANE ANCHOR containing ephrin found in developing tectum. It has been shown to mediate the bundling of cortical axons and repel the axonal growth of retinal ganglia axons. It is found in a variety of adult tissues of BRAIN; HEART; and KIDNEY.
An ephrin that was originally identified as the product of an early response gene induced by TUMOR NECROSIS FACTORS. It is linked to the CELL MEMBRANE via a GLYCOINOSITOL PHOSPHOLIPID MEMBRANE ANCHOR and binds EPHA2 RECEPTOR with high affinity. During embryogenesis high levels of ephrin-A1 are expressed in LUNG; KIDNEY; SALIVARY GLANDS; and INTESTINE.
A GLYCOINOSITOL PHOSPHOLIPID MEMBRANE ANCHOR containing ephrin found in variety of adult tissue such as KIDNEY; LUNG; COLON and OVARY. During embryonic development, ephrin-A4 is expressed in the HIPPOCAMPUS and CEREBRAL CORTEX. It binds preferentially to ephA receptors (EPH FAMILY RECEPTORS) with the exception of the EPHA1 RECEPTOR.
An eph family receptor found in variety of tissues including BRAIN. During embryogenesis, EphA4 receptor exhibits a diverse spatial and temporal patterns of expression suggesting its role in multiple developmental processes.
A GLYCOINOSITOL PHOSPHOLIPID MEMBRANE ANCHOR-containing ephrin with a high affinity for the EPHA3 RECEPTOR. Early in embryogenesis it is expressed at high levels in the MESENCEPHALON; SOMITES; branchial arches, and LIMB BUDS.
The founding member of the EPH FAMILY RECEPTORS. It was first cloned from an erythropoietin-producing human hepatocellular carcinoma cell line and is highly conserved among many mammalian species. Overproduction of the EphA1 receptor is associated with tumors and tumor cells of epithelial origin. It is also expressed at high levels in LIVER; LUNG; and KIDNEY; which is in contrast to many other members of the Eph receptor that are found primarily in tissues of the nervous system.
A transmembrane domain containing ephrin. Although originally found to be specific for the EPHB3 RECEPTOR it has since been shown to bind a variety of EPH FAMILY RECEPTORS. During embryogenesis ephrin-B3 is expressed at high levels in the ventral neural tube. In adult tissues, it is found primarily in the BRAIN and HEART.
An eph family receptor found in a variety of adult and embryonic tissues. Unlike the majority of proteins in this class there is little or no expression of EphB4 receptor in the BRAIN. It has been found at high levels in developing mammary glands and in invasive mammary tumors.
A GLYCOINOSITOL PHOSPHOLIPID MEMBRANE ANCHOR containing ephrin with a high affinity for the EPHA3 RECEPTOR; EPHA5 RECEPTOR; EPHA6 RECEPTOR; EPHA7 RECEPTOR; and EPHA8 RECEPTOR. It is found primarily in NERVE TISSUE.
An eph family receptor that is found primarily in adult BRAIN and variety of tissues in the developing embryo tissues. During embryonic development high levels of EphA3 receptor expression is seen in the nervous system and coincides with neuronal cell migration, suggesting a role for this protein in axonal pathfinding.
An eph family receptor found widely expressed in embryonic and adult tissues. High levels of EphB2 receptor are observed in growing AXONS and NERVE FIBERS. Several isoforms of the protein exist due to multiple alternative mRNA splicing.
An Eph family receptor found abundantly in tissues of epithelial origin. It is expressed in a diverse array of tissues during embryonic development, suggesting that it may play a role in embryogenesis. In adult tissues high levels of the receptor are expressed in the LUNG; SKIN; SMALL INTESTINE and OVARY.
An eph family receptor found primarily in differentiated neuronal tissues. Several isoforms of EphA5 receptor occur due to multiple alternative RNA splicing. The protein is prominently expressed in the NEURONS of the LIMBIC SYSTEM during development and throughout adult life, suggesting its role in the plasticity of limbic structure and function.
An eph family receptor found widely expressed in embryo tissues, including the NERVOUS SYSTEM. In the BRAIN high levels of EphA7 expression occurs in the anterior tectum, medulla, RHOMBENCEPHALON, and SUBCOMMISSURAL ORGAN. Several isoforms of the protein occur due to multiple alternative spicing of the EphA7 mRNA.
An eph family receptor found in a number of tissues including BRAIN; LUNG; KIDNEY; PANCREAS; INTESTINE; and HEART. During embryogenesis EphB3 receptor is expressed at high levels in the brain.
An eph family receptor found primarily in the nervous system. In the embryonic BRAIN EphB1 receptor expression occurs in the mantle layer and increases with the progression of embryogenesis. In adult brain it is found in the several regions including the CEREBELLUM; CEREBRAL CORTEX; and CAUDATE NUCLEUS; and PUTAMEN.
The intracellular transfer of information (biological activation/inhibition) through a signal pathway. In each signal transduction system, an activation/inhibition signal from a biologically active molecule (hormone, neurotransmitter) is mediated via the coupling of a receptor/enzyme to a second messenger system or to an ion channel. Signal transduction plays an important role in activating cellular functions, cell differentiation, and cell proliferation. Examples of signal transduction systems are the GAMMA-AMINOBUTYRIC ACID-postsynaptic receptor-calcium ion channel system, the receptor-mediated T-cell activation pathway, and the receptor-mediated activation of phospholipases. Those coupled to membrane depolarization or intracellular release of calcium include the receptor-mediated activation of cytotoxic functions in granulocytes and the synaptic potentiation of protein kinase activation. Some signal transduction pathways may be part of larger signal transduction pathways; for example, protein kinase activation is part of the platelet activation signal pathway.
The anterior aspect of the casing that surrounds the natural CRYSTALLINE LENS.
A subtype of non-receptor protein tyrosine phosphatases that is characterized by the presence of an amino-terminal FERM domain, an intervening region containing five different PDZ domains, and a carboxyl-terminal phosphatase domain. In addition to playing a role as a regulator of the FAS RECEPTOR activity this subtype interacts via its PDZ and FERM domains with a variety of INTRACELLULAR SIGNALING PROTEINS and CYTOSKELETAL PROTEINS.
An eph family receptor found primarily in BRAIN and THYMUS. The EphB6 receptor is unusual in that its tyrosine kinase domain shares little homology with other members of this class. The unusual tyrosine kinase domain of this receptor appears to result in its lack of tyrosine kinase activity.
An eph family receptor found exclusively in BRAIN. EphA8 receptors may play a role in the axonal guidance of a subset of tectal commissural NEURONS.
Bulbous enlargement of the growing tip of nerve axons and dendrites. They are crucial to neuronal development because of their pathfinding ability and their role in synaptogenesis.
A molecule that binds to another molecule, used especially to refer to a small molecule that binds specifically to a larger molecule, e.g., an antigen binding to an antibody, a hormone or neurotransmitter binding to a receptor, or a substrate or allosteric effector binding to an enzyme. Ligands are also molecules that donate or accept a pair of electrons to form a coordinate covalent bond with the central metal atom of a coordination complex. (From Dorland, 27th ed)
A 120-kDa RAS GTPase-activating protein that binds to tyrosine phosphoproteins through its SH2 domains. The 100-kDa RNA-splicing variant (p100 GAP protein) is expressed in placenta.
Nerve fibers that are capable of rapidly conducting impulses away from the neuron cell body.
The development of anatomical structures to create the form of a single- or multi-cell organism. Morphogenesis provides form changes of a part, parts, or the whole organism.
A class of cellular receptors that have an intrinsic PROTEIN-TYROSINE KINASE activity.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action during the developmental stages of an organism.
The anatomical parts that make up an organism in the early stages of development.
Proteins which are found in membranes including cellular and intracellular membranes. They consist of two types, peripheral and integral proteins. They include most membrane-associated enzymes, antigenic proteins, transport proteins, and drug, hormone, and lectin receptors.
The processes occurring in early development that direct morphogenesis. They specify the body plan ensuring that cells will proceed to differentiate, grow, and diversify in size and shape at the correct relative positions. Included are axial patterning, segmentation, compartment specification, limb position, organ boundary patterning, blood vessel patterning, etc.
The movement of cells from one location to another. Distinguish from CYTOKINESIS which is the process of dividing the CYTOPLASM of a cell.
The anterior subdivision of the embryonic PROSENCEPHALON or the corresponding part of the adult prosencephalon that includes the cerebrum and associated structures.
A derivative of benzodiazepine that acts on the cholecystokinin A (CCKA) receptor to antagonize CCK-8's (SINCALIDE) physiological and behavioral effects, such as pancreatic stimulation and inhibition of feeding.
Quinolinium compounds are organic salts formed by the protonation of quinoline, characterized by a positively charged nitrogen atom surrounded by an aromatic ring, which have been used in various applications including as antimicrobial agents and chemical research.
A species of HENIPAVIRUS, closely related to HENDRA VIRUS, which emerged in Peninsular Malaysia in 1998. It causes a severe febrile VIRAL ENCEPHALITIS in humans and also encephalitis and RESPIRATORY TRACT INFECTIONS in pigs. Fruit bats (PTEROPUS) are the natural host.
The posterior of the three primitive cerebral vesicles of an embryonic brain. It consists of myelencephalon, metencephalon, and isthmus rhombencephali from which develop the major BRAIN STEM components, such as MEDULLA OBLONGATA from the myelencephalon, CEREBELLUM and PONS from the metencephalon, with the expanded cavity forming the FOURTH VENTRICLE.
The only species of a cosmopolitan ascidian.
A variation of the PCR technique in which cDNA is made from RNA via reverse transcription. The resultant cDNA is then amplified using standard PCR protocols.
A technique that localizes specific nucleic acid sequences within intact chromosomes, eukaryotic cells, or bacterial cells through the use of specific nucleic acid-labeled probes.
Adherence of cells to surfaces or to other cells.
Paired, segmented masses of MESENCHYME located on either side of the developing spinal cord (neural tube). Somites derive from PARAXIAL MESODERM and continue to increase in number during ORGANOGENESIS. Somites give rise to SKELETON (sclerotome); MUSCLES (myotome); and DERMIS (dermatome).
The developmental entity of a fertilized egg (ZYGOTE) in animal species other than MAMMALS. For chickens, use CHICK EMBRYO.
The entire nerve apparatus, composed of a central part, the brain and spinal cord, and a peripheral part, the cranial and spinal nerves, autonomic ganglia, and plexuses. (Stedman, 26th ed)
The developmental entity of a fertilized chicken egg (ZYGOTE). The developmental process begins about 24 h before the egg is laid at the BLASTODISC, a small whitish spot on the surface of the EGG YOLK. After 21 days of incubation, the embryo is fully developed before hatching.
Laboratory mice that have been produced from a genetically manipulated EGG or EMBRYO, MAMMALIAN.
Bone-forming cells which secrete an EXTRACELLULAR MATRIX. HYDROXYAPATITE crystals are then deposited into the matrix to form bone.
The simultaneous or sequential binding of multiple cell surface receptors to different ligands resulting in coordinated stimulation or suppression of signal transduction.
Cells propagated in vitro in special media conducive to their growth. Cultured cells are used to study developmental, morphologic, metabolic, physiologic, and genetic processes, among others.
Histochemical localization of immunoreactive substances using labeled antibodies as reagents.
The anterior pair of the quadrigeminal bodies which coordinate the general behavioral orienting responses to visual stimuli, such as whole-body turning, and reaching.
An exotic species of the family CYPRINIDAE, originally from Asia, that has been introduced in North America. They are used in embryological studies and to study the effects of certain chemicals on development.
The SKELETON of the HEAD including the FACIAL BONES and the bones enclosing the BRAIN.
A c-jun amino-terminal kinase that is activated by environmental stress and pro-inflammatory cytokines. Several isoforms of the protein with molecular sizes of 48 and 54 KD exist due to multiple ALTERNATIVE SPLICING.
RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm.
The vessels carrying blood away from the capillary beds.
Strains of mice in which certain GENES of their GENOMES have been disrupted, or "knocked-out". To produce knockouts, using RECOMBINANT DNA technology, the normal DNA sequence of the gene being studied is altered to prevent synthesis of a normal gene product. Cloned cells in which this DNA alteration is successful are then injected into mouse EMBRYOS to produce chimeric mice. The chimeric mice are then bred to yield a strain in which all the cells of the mouse contain the disrupted gene. Knockout mice are used as EXPERIMENTAL ANIMAL MODELS for diseases (DISEASE MODELS, ANIMAL) and to clarify the functions of the genes.
The process in which substances, either endogenous or exogenous, bind to proteins, peptides, enzymes, protein precursors, or allied compounds. Specific protein-binding measures are often used as assays in diagnostic assessments.
The introduction of a phosphoryl group into a compound through the formation of an ester bond between the compound and a phosphorus moiety.
The basic cellular units of nervous tissue. Each neuron consists of a body, an axon, and dendrites. Their purpose is to receive, conduct, and transmit impulses in the NERVOUS SYSTEM.
The ten-layered nervous tissue membrane of the eye. It is continuous with the OPTIC NERVE and receives images of external objects and transmits visual impulses to the brain. Its outer surface is in contact with the CHOROID and the inner surface with the VITREOUS BODY. The outer-most layer is pigmented, whereas the inner nine layers are transparent.
Neurons of the innermost layer of the retina, the internal plexiform layer. They are of variable sizes and shapes, and their axons project via the OPTIC NERVE to the brain. A small subset of these cells act as photoreceptors with projections to the SUPRACHIASMATIC NUCLEUS, the center for regulating CIRCADIAN RHYTHM.
The flexible rope-like structure that connects a developing FETUS to the PLACENTA in mammals. The cord contains blood vessels which carry oxygen and nutrients from the mother to the fetus and waste products away from the fetus.
The level of protein structure in which combinations of secondary protein structures (alpha helices, beta sheets, loop regions, and motifs) pack together to form folded shapes called domains. Disulfide bridges between cysteines in two different parts of the polypeptide chain along with other interactions between the chains play a role in the formation and stabilization of tertiary structure. Small proteins usually consist of only one domain but larger proteins may contain a number of domains connected by segments of polypeptide chain which lack regular secondary structure.
Inbred C57BL mice are a strain of laboratory mice that have been produced by many generations of brother-sister matings, resulting in a high degree of genetic uniformity and homozygosity, making them widely used for biomedical research, including studies on genetics, immunology, cancer, and neuroscience.
Any of several ways in which living cells of an organism communicate with one another, whether by direct contact between cells or by means of chemical signals carried by neurotransmitter substances, hormones, and cyclic AMP.
Theoretical representations that simulate the behavior or activity of biological processes or diseases. For disease models in living animals, DISEASE MODELS, ANIMAL is available. Biological models include the use of mathematical equations, computers, and other electronic equipment.
Progressive restriction of the developmental potential and increasing specialization of function that leads to the formation of specialized cells, tissues, and organs.
The phenotypic manifestation of a gene or genes by the processes of GENETIC TRANSCRIPTION and GENETIC TRANSLATION.
A technique in which electric pulses of intensity in kilovolts per centimeter and of microsecond-to-millisecond duration cause a temporary loss of the semipermeability of CELL MEMBRANES, thus leading to ion leakage, escape of metabolites, and increased uptake by cells of drugs, molecular probes, and DNA.
The two longitudinal ridges along the PRIMITIVE STREAK appearing near the end of GASTRULATION during development of nervous system (NEURULATION). The ridges are formed by folding of NEURAL PLATE. Between the ridges is a neural groove which deepens as the fold become elevated. When the folds meet at midline, the groove becomes a closed tube, the NEURAL TUBE.
Methods used for detecting the amplified DNA products from the polymerase chain reaction as they accumulate instead of at the end of the reaction.
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Techniques to alter a gene sequence that result in an inactivated gene, or one in which the expression can be inactivated at a chosen time during development to study the loss of function of a gene.
A large multinuclear cell associated with the BONE RESORPTION. An odontoclast, also called cementoclast, is cytomorphologically the same as an osteoclast and is involved in CEMENTUM resorption.
A positive regulatory effect on physiological processes at the molecular, cellular, or systemic level. At the molecular level, the major regulatory sites include membrane receptors, genes (GENE EXPRESSION REGULATION), mRNAs (RNA, MESSENGER), and proteins.
Proteins obtained from the ZEBRAFISH. Many of the proteins in this species have been the subject of studies involving basic embryological development (EMBRYOLOGY).
Venous vessels in the umbilical cord. They carry oxygenated, nutrient-rich blood from the mother to the FETUS via the PLACENTA. In humans, there is normally one umbilical vein.
The process of bone formation. Histogenesis of bone including ossification.
A family of conserved cell surface receptors that contain EPIDERMAL GROWTH FACTOR repeats in their extracellular domain and ANKYRIN repeats in their cytoplasmic domains. The cytoplasmic domain of notch receptors is released upon ligand binding and translocates to the CELL NUCLEUS where it acts as transcription factor.
A cell line derived from cultured tumor cells.
The development of new BLOOD VESSELS during the restoration of BLOOD CIRCULATION during the healing process.
A species of nematode that is widely used in biological, biochemical, and genetic studies.
An intermediate filament protein found only in glial cells or cells of glial origin. MW 51,000.
Protein analogs and derivatives of the Aequorea victoria green fluorescent protein that emit light (FLUORESCENCE) when excited with ULTRAVIOLET RAYS. They are used in REPORTER GENES in doing GENETIC TECHNIQUES. Numerous mutants have been made to emit other colors or be sensitive to pH.
Established cell cultures that have the potential to propagate indefinitely.
The degree of similarity between sequences of amino acids. This information is useful for the analyzing genetic relatedness of proteins and species.
Small double-stranded, non-protein coding RNAs (21-31 nucleotides) involved in GENE SILENCING functions, especially RNA INTERFERENCE (RNAi). Endogenously, siRNAs are generated from dsRNAs (RNA, DOUBLE-STRANDED) by the same ribonuclease, Dicer, that generates miRNAs (MICRORNAS). The perfect match of the siRNAs' antisense strand to their target RNAs mediates RNAi by siRNA-guided RNA cleavage. siRNAs fall into different classes including trans-acting siRNA (tasiRNA), repeat-associated RNA (rasiRNA), small-scan RNA (scnRNA), and Piwi protein-interacting RNA (piRNA) and have different specific gene silencing functions.
Identification of proteins or peptides that have been electrophoretically separated by blot transferring from the electrophoresis gel to strips of nitrocellulose paper, followed by labeling with antibody probes.
Any detectable and heritable change in the genetic material that causes a change in the GENOTYPE and which is transmitted to daughter cells and to succeeding generations.
The study of crystal structure using X-RAY DIFFRACTION techniques. (McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control of gene action in neoplastic tissue.
Mice bearing mutant genes which are phenotypically expressed in the animals.
All of the processes involved in increasing CELL NUMBER including CELL DIVISION.
Any of the processes by which nuclear, cytoplasmic, or intercellular factors influence the differential control (induction or repression) of gene action at the level of transcription or translation.
A technique of culturing mixed cell types in vitro to allow their synergistic or antagonistic interactions, such as on CELL DIFFERENTIATION or APOPTOSIS. Coculture can be of different types of cells, tissues, or organs from normal or disease states.
A tumor necrosis factor receptor subtype that is expressed primarily in IMMUNE SYSTEM cells. It has specificity for membrane-bound form of TUMOR NECROSIS FACTORS and mediates intracellular-signaling through TNF RECEPTOR ASSOCIATED FACTORS.
The thin layer of GRAY MATTER on the surface of the CEREBRAL HEMISPHERES that develops from the TELENCEPHALON and folds into gyri and sulchi. It reaches its highest development in humans and is responsible for intellectual faculties and higher mental functions.
A multi-functional catenin that participates in CELL ADHESION and nuclear signaling. Beta catenin binds CADHERINS and helps link their cytoplasmic tails to the ACTIN in the CYTOSKELETON via ALPHA CATENIN. It also serves as a transcriptional co-activator and downstream component of WNT PROTEIN-mediated SIGNAL TRANSDUCTION PATHWAYS.
A secreted matrix metalloproteinase that plays a physiological role in the degradation of extracellular matrix found in skeletal tissues. It is synthesized as an inactive precursor that is activated by the proteolytic cleavage of its N-terminal propeptide.
Highly specialized EPITHELIAL CELLS that line the HEART; BLOOD VESSELS; and lymph vessels, forming the ENDOTHELIUM. They are polygonal in shape and joined together by TIGHT JUNCTIONS. The tight junctions allow for variable permeability to specific macromolecules that are transported across the endothelial layer.
Renewal or physiological repair of damaged nerve tissue.
Recombinant proteins produced by the GENETIC TRANSLATION of fused genes formed by the combination of NUCLEIC ACID REGULATORY SEQUENCES of one or more genes with the protein coding sequences of one or more genes.
The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.
Proteins and peptides that are involved in SIGNAL TRANSDUCTION within the cell. Included here are peptides and proteins that regulate the activity of TRANSCRIPTION FACTORS and cellular processes in response to signals from CELL SURFACE RECEPTORS. Intracellular signaling peptide and proteins may be part of an enzymatic signaling cascade or act through binding to and modifying the action of other signaling factors.
Cells that line the inner and outer surfaces of the body by forming cellular layers (EPITHELIUM) or masses. Epithelial cells lining the SKIN; the MOUTH; the NOSE; and the ANAL CANAL derive from ectoderm; those lining the RESPIRATORY SYSTEM and the DIGESTIVE SYSTEM derive from endoderm; others (CARDIOVASCULAR SYSTEM and LYMPHATIC SYSTEM) derive from mesoderm. Epithelial cells can be classified mainly by cell shape and function into squamous, glandular and transitional epithelial cells.
Calcium-dependent cell adhesion proteins. They are important in the formation of ADHERENS JUNCTIONS between cells. Cadherins are classified by their distinct immunological and tissue specificities, either by letters (E- for epithelial, N- for neural, and P- for placental cadherins) or by numbers (cadherin-12 or N-cadherin 2 for brain-cadherin). Cadherins promote cell adhesion via a homophilic mechanism as in the construction of tissues and of the whole animal body.
A species of CERCOPITHECUS containing three subspecies: C. tantalus, C. pygerythrus, and C. sabeus. They are found in the forests and savannah of Africa. The African green monkey (C. pygerythrus) is the natural host of SIMIAN IMMUNODEFICIENCY VIRUS and is used in AIDS research.
The determination of the pattern of genes expressed at the level of GENETIC TRANSCRIPTION, under specific circumstances or in a specific cell.
Refers to animals in the period of time just after birth.
Endogenous substances, usually proteins, which are effective in the initiation, stimulation, or termination of the genetic transcription process.
The outward appearance of the individual. It is the product of interactions between genes, and between the GENOTYPE and the environment.
A pathologic process consisting of the proliferation of blood vessels in abnormal tissues or in abnormal positions.

Ephrin-dependent growth and pruning of hippocampal axons. (1/117)

Neuronal connections are arranged topographically such that the spatial organization of neurons is preserved by their termini in the targets. During the development of topographic projections, axons initially explore areas much wider than the final targets, and mistargeted axons are pruned later. The molecules regulating these processes are not known. We report here that the ligands of the Eph family tyrosine kinase receptors may regulate both the initial outgrowth and the subsequent pruning of axons. In the presence of ephrins, the outgrowth and branching of the receptor-positive hippocampal axons are enhanced. However, these axons are induced later to degenerate. These observations suggest that the ephrins and their receptors may regulate topographic map formation by stimulating axonal arborization and by pruning mistargeted axons.  (+info)

Modulation of EphA receptor function by coexpressed ephrinA ligands on retinal ganglion cell axons. (2/117)

The Eph family is thought to exert its function through the complementary expression of receptors and ligands. Here, we show that EphA receptors colocalize on retinal ganglion cell (RGC) axons with EphA ligands, which are expressed in a high-nasal-to-low-temporal pattern. In the stripe assay, only temporal axons are normally sensitive for repellent axon guidance cues of the caudal tectum. However, overexpression of ephrinA ligands on temporal axons abolishes this sensitivity, whereas treatment with PI-PLC both removes ephrinA ligands from retinal axons and induces a striped outgrowth of formerly insensitive nasal axons. In vivo, retinal overexpression of ephrinA2 leads to topographic targeting errors of temporal axons. These data suggest that differential ligand expression on retinal axons is a major determinant of topographic targeting in the retinotectal projection.  (+info)

Elf-1 and PU.1 induce expression of gp91(phox) via a promoter element mutated in a subset of chronic granulomatous disease patients. (3/117)

The cytochrome b heavy chain (gp91(phox)) is the redox center of the NADPH-oxidase and is highly expressed in mature myeloid cells. Point mutations at -57, -55, -53, and -52 bp of the gp91(phox) promoter have been detected in patients with chronic granulomatous disease (CGD; Newburger et al, J Clin Invest 94:1205, 1994; and Suzuki et al, Proc Natl Acad Sci USA 95:6085, 1998). We report that Elf-1 and PU. 1, ets family members highly expressed in myeloid cells, bind to this promoter element. Either factor trans-activates the -102 to +12 bp gp91(phox) promoter when overexpressed in nonhematopoietic HeLa cells or the PLB985 myeloid cell line. However, no synergy of gp91(phox) promoter activation occurs when both Elf-1 and PU.1 are overexpressed. Introduction of the -57 bp or -55 bp CGD mutations into the gp91(phox) promoter significantly reduces the binding affinity of Elf-1 and PU.1 and also reduces the ability of these factors to trans-activate the promoter. These results indicate that Elf-1 and PU.1 contribute to directing the lineage-restricted expression of the gp91(phox) gene in phagocytes and that failure of these factors to effectively interact with this promoter results in CGD.  (+info)

Requirement for the zebrafish mid-hindbrain boundary in midbrain polarisation, mapping and confinement of the retinotectal projection. (4/117)

The organizer at the midbrain-hindbrain boundary (MHB organizer) has been proposed to induce and polarize the midbrain during development. We investigate the requirement for the MHB organizer in acerebellar mutants, which lack a MHB and cerebellum, but retain a tectum, and are mutant for fgf8, a candidate inducer and polarizer. We examine the retinotectal projection in the mutants to assay polarity in the tectum. In mutant tecta, retinal ganglion cell (RGC) axons form overlapping termination fields, especially in the ventral tectum, and along both the anterior-posterior and dorsal-ventral axis of the tectum, consistent with a MHB requirement in generating midbrain polarity. However, polarity is not completely lost in the mutant tecta, in spite of the absence of the MHB. Moreover, graded expression of the ephrin family ligand Ephrin-A5b is eliminated, whereas Ephrin-A2 and Ephrin-A5a expression is leveled in acerebellar mutant tecta, showing that ephrins are differentially affected by the absence of the MHB. Some RGC axons overshoot beyond the mutant tectum, suggesting that the MHB also serves a barrier function for axonal growth. By transplanting whole eye primordia, we show that mapping defects and overshooting largely, but not exclusively, depend on tectal, but not retinal genotype, and thus demonstrate an independent function for Fgf8 in retinal development. The MHB organizer, possibly via Fgf8 itself, is thus required for midbrain polarisation and for restricting axonal growth, but other cell populations may also influence midbrain polarity.  (+info)

Ephrin-A binding and EphA receptor expression delineate the matrix compartment of the striatum. (5/117)

The striatum integrates limbic and neocortical inputs to regulate sensorimotor and psychomotor behaviors. This function is dependent on the segregation of striatal projection neurons into anatomical and functional components, such as the striosome and matrix compartments. In the present study the association of ephrin-A cell surface ligands and EphA receptor tyrosine kinases (RTKs) with the organization of these compartments was determined in postnatal rats. Ephrin-A1 and ephrin-A4 selectively bind to EphA receptors on neurons restricted to the matrix compartment. Binding is absent from the striosomes, which were identified by mu-opioid receptor immunostaining. In contrast, ephrin-A2, ephrin-A3, and ephrin-A5 exhibit a different mosaic binding pattern that appears to define a subset of matrix neurons. In situ hybridization for EphA RTKs reveals that the two different ligand binding patterns strictly match the mRNA expression patterns of EphA4 and EphA7. Ligand-receptor binding assays indicate that ephrin-A1 and ephrin-A4 selectively bind EphA4 but not EphA7 in the lysates of striatal tissue. Conversely, ephrin-A2, ephrin-A3, and ephrin-A5 bind EphA7 but not EphA4. These observations implicate selective interactions between ephrin-A molecules and EphA RTKs as potential mechanisms for regulating the compartmental organization of the striatum.  (+info)

The transcription factors Elf-1 and GATA-1 bind to cell-specific enhancer elements of human high-affinity IgE receptor alpha-chain gene. (6/117)

Key regulatory regions necessary for the expression of the gene encoding FcepsilonRI alpha-chain, a component of the high-affinity IgE receptor primarily responsible for IgE-dependent allergic response, were investigated. Two regions, -74/-69 and -55/-47, which contained binding motifs for proteins belonging to the Ets family and the GATA family, respectively, were shown to be necessary for the activation of the alpha-chain promoter. Both the regulatory elements enhanced the promoter activity only in alpha-chain-producing cells PT18 and RBL-2H3 (mast cell lines), indicating that the elements required specific trans-acting proteins present in the alpha-chain-producing cells. EMSA using nuclear extracts and in vitro-translated proteins revealed that Elf-1 and GATA-1 bound to the enhancer elements. This is the first report describing the regulation in the expression of the FcepsilonRI alpha-chain.  (+info)

Myeloid ELF-1-like factor up-regulates lysozyme transcription in epithelial cells. (7/117)

Lysozyme is an important component of innate immunity against common pathogens at mucosal surfaces. We previously cloned and characterized the bovine lysozyme 5A (lys5A) promoter with the purpose of determining cis- and trans-acting elements controlling airway epithelial cell-specific expression. We found that such expression is controlled by protein binding to an ETS consensus sequence located approximately at -46 to -40 bp from the transcription start site. The identity of the ETS-related protein responsible for gene transactivation was unknown. In this study, we screened six ETS-related proteins by transient transfection into epithelial cells and fibroblasts. Results showed that among these factors, the myeloid Elf-1-like factor (MEF) was the most potent. Gel shift analysis of epithelial cell nuclear extracts using a lys5A probe including the ETS-binding site (-50/-31) yielded a single band with retarded mobility. This band was supershifted by an antibody directed against MEF. Supporting the possibility that MEF is responsible for functional transactivation of lysozyme in epithelial cells, we found that antisense MEF mRNA decreased lys5A promoter activity and that MEF overexpression in stably transfected cells increased lysozyme mRNA and protein expression. We conclude that MEF is required for epithelial cell transactivation of lysozyme.  (+info)

Cell autonomous and non-cell autonomous functions of Otx2 in patterning the rostral brain. (8/117)

Previous studies have shown that the homeobox gene Otx2 is required first in the visceral endoderm for induction of forebrain and midbrain, and subsequently in the neurectoderm for its regional specification. Here, we demonstrate that Otx2 functions both cell autonomously and non-cell autonomously in neurectoderm cells of the forebrain and midbrain to regulate expression of region-specific homeobox and cell adhesion genes. Using chimeras containing both Otx2 mutant and wild-type cells in the brain, we observe a reduction or loss of expression of Rpx/Hesx1, Wnt1, R-cadherin and ephrin-A2 in mutant cells, whereas expression of En2 and Six3 is rescued by surrounding wild-type cells. Forebrain Otx2 mutant cells subsequently undergo apoptosis. Altogether, this study demonstrates that Otx2 is an important regulator of brain patterning and morphogenesis, through its regulation of candidate target genes such as Rpx/Hesx1, Wnt1, R-cadherin and ephrin-A2.  (+info)

Ephrins are a family of membrane-bound proteins that play crucial roles in various biological processes, including cell migration, axon guidance, and tissue boundary formation during embryonic development. They interact with Eph receptors, which are tyrosine kinase receptors found on the surface of neighboring cells. This interaction results in bidirectional signaling between the two cells, affecting their behaviors and influencing the organization of tissues and organs.

There are two main types of ephrins: Ephrin-A (also known as GPI-anchored ephrins) and Ephrin-B (transmembrane ephrins). Ephrin-A proteins are attached to the cell membrane through a glycosylphosphatidylinositol (GPI) anchor, while Ephrin-B proteins have a transmembrane domain and a cytoplasmic tail. Both types of ephrins interact with Eph receptors, leading to the initiation of intracellular signaling cascades that regulate various cellular responses.

Dysregulation of ephrin/Eph receptor interactions has been implicated in several human diseases, including cancer, where they can contribute to tumor growth, progression, and metastasis. Therefore, understanding the functions and regulation of ephrins and their receptors is essential for developing novel therapeutic strategies to treat various diseases.

Eph family receptors are a group of tyrosine kinase receptors that play crucial roles in the development and function of the nervous system, as well as in other tissues. They are named after the first discovered member of this family, EPH (Erythropoietin-Producing Human Hepatocellular carcinoma) receptor.

These receptors are divided into two subfamilies: EphA and EphB, based on their binding preferences for ephrin ligands. Ephrins are membrane-bound proteins that can be either GPI-anchored (ephrin-A) or transmembrane (ephrin-B), and they interact with Eph receptors in a bidirectional manner, activating both forward signaling in the receptor-expressing cell and reverse signaling in the ephrin-expressing cell.

Eph receptors and ephrins are essential for axon guidance, topographic mapping, and synaptic plasticity during neural development. They also participate in various processes in adult tissues, such as angiogenesis, tumorigenesis, and immune responses. Dysregulation of Eph family receptors has been implicated in several diseases, including cancer, neurological disorders, and vascular diseases.

Ephrin-B2 is a type of protein that belongs to the ephrin family and is primarily involved in the development and function of the nervous system. It is a membrane-bound ligand for Eph receptor tyrosine kinases, and their interactions play crucial roles in cell-cell communication during embryogenesis and adult tissue homeostasis.

Ephrin-B2 is specifically a glycosylphosphatidylinositol (GPI)-anchored protein that is expressed on the cell membrane of various cell types, including endothelial cells, neurons, and some immune cells. Its interactions with Eph receptors, which are transmembrane proteins, lead to bidirectional signaling across the contacting cell membranes. This process regulates various aspects of cell behavior, such as adhesion, migration, repulsion, and proliferation.

In the context of the cardiovascular system, ephrin-B2 is essential for the development and maintenance of blood vessels. It is involved in the formation of arterial-venous boundaries, vascular branching, and remodeling. Mutations or dysregulation of ephrin-B2 have been implicated in various diseases, including cancer, where it can contribute to tumor angiogenesis and metastasis.

Ephrin-B1 is a type of protein that belongs to the ephrin family and is involved in cell signaling, specifically in the process known as cell-cell communication. It is a transmembrane protein, which means it spans the membrane of the cell and has a portion that faces the outside of the cell (the extracellular domain) and a portion that faces the inside of the cell (the intracellular domain).

Ephrin-B1 binds to Eph receptors, which are tyrosine kinase receptors found on the surface of neighboring cells. This binding results in the initiation of a signaling cascade that can influence various cellular processes, including cell migration, adhesion, and proliferation.

Ephrin-B1 is widely expressed in various tissues throughout the body, including the nervous system, where it plays important roles in the development and function of the brain. Mutations in the gene that encodes ephrin-B1 have been associated with certain neurological disorders, such as intellectual disability and epilepsy.

Ephrin-A5 is a type of protein that belongs to the ephrin family. Ephrins are membrane-bound proteins that interact with Eph receptors, which are tyrosine kinase receptors found on the surface of cells. The interaction between ephrins and Eph receptors plays a crucial role in the development and function of the nervous system, including axon guidance, cell migration, and synaptic plasticity.

Ephrin-A5 is specifically classified as a glycosylphosphatidylinositol (GPI)-anchored protein, which means it is attached to the outer layer of the cell membrane through a GPI anchor. It is primarily expressed in various tissues, including the brain, heart, and lungs.

In the nervous system, Ephrin-A5 and its receptor, EphA4, are involved in repulsive guidance cues that help to establish proper neuronal connections during development. Dysregulation of this interaction has been implicated in several neurological disorders, such as spinal cord injuries, Alzheimer's disease, and schizophrenia.

Ephrin-A1 is a type of protein that belongs to the ephrin family. It is a membrane-bound ligand for Eph receptors, which are tyrosine kinase receptors located on the cell surface. Ephrin-A1 and its receptors play critical roles in various biological processes, including cell migration, axon guidance, and tissue boundary formation during embryonic development. Ephrin-A1 is also involved in angiogenesis, tumorigenesis, and metastasis in cancer. It is encoded by the EFNAs gene in humans.

Ephrin-A4 is a type of protein that belongs to the ephrin family. Ephrins are membrane-bound proteins that play crucial roles in various biological processes, including cell signaling and communication during development. Specifically, Ephrin-A4 is a ligand for Eph receptors, which are tyrosine kinase receptors located on the cell membrane.

Ephrin-A4 is composed of a glycosylphosphatidylinositol (GPI) anchor that attaches it to the cell membrane and an extracellular domain that interacts with Eph receptors. When Ephrin-A4 binds to an Eph receptor on a neighboring cell, it triggers a cascade of intracellular signaling events that can regulate various cellular processes, such as cell adhesion, migration, and proliferation.

In the medical field, Ephrin-A4 has been studied in the context of various diseases, including cancer. For example, abnormal expression of Ephrin-A4 has been observed in several types of tumors, and it has been suggested to play a role in tumor progression and metastasis. However, more research is needed to fully understand the functional significance of Ephrin-A4 in health and disease.

EphA4 is a type of receptor tyrosine kinase that belongs to the Eph (Erythropoietin-producing hepatocellular) family of receptors. It is a transmembrane protein found on the surface of various types of cells, including neurons and glial cells in the nervous system.

EphA4 receptors play critical roles in several biological processes, such as cell migration, axon guidance, and synaptic plasticity during development and throughout adulthood. They interact with ephrin proteins, which are ligands (molecules that bind to receptors) found on adjacent cells. The interaction between EphA4 and ephrins triggers a cascade of intracellular signaling events that ultimately influence cell behavior.

In summary, EphA4 is a type of receptor involved in cell-cell communication, particularly during the development and functioning of the nervous system. Its dysfunction has been implicated in several neurological disorders, such as spinal cord injuries, Alzheimer's disease, and various forms of cancer.

Ephrin-A2 is a type of protein that belongs to the ephrin family. It is a membrane-bound ligand for Eph receptors, which are tyrosine kinase receptors located on the cell surface. Ephrin-A2 and Eph receptors play critical roles in various biological processes, including axon guidance, tissue boundary formation, and tumorigenesis.

Ephrin-A2 is encoded by the EFNB2 gene and is expressed on the cell membrane as a glycosylphosphatidylinositol (GPI)-anchored protein. It can interact with several Eph receptors, including EphA3, EphA4, EphA5, and EphA7, leading to bidirectional signaling that regulates cell-cell interactions and communication.

In the nervous system, ephrin-A2 and its receptors are essential for the development and maintenance of neural circuits. They help to establish precise connections between neurons by mediating repulsive interactions that guide axon growth and fasciculation. Additionally, ephrin-A2 has been implicated in various pathological conditions, such as cancer, where it can contribute to tumor progression and metastasis.

EphA1 is a type of receptor tyrosine kinase (RTK) that belongs to the Eph family of receptors. It is a single-pass transmembrane protein that contains an extracellular domain with a binding site for its ligand, ephrin-A5, and an intracellular domain with tyrosine kinase activity.

EphA1 receptors are involved in various biological processes, including cell migration, axon guidance, and tissue boundary formation during embryonic development. They also play a role in angiogenesis, neuroprotection, and tumorigenesis in adults.

The binding of ephrin-A5 to EphA1 receptors triggers bidirectional signaling, affecting both the receptor-expressing cell and the ephrin-presenting cell. This interaction can lead to repulsion, adhesion, or collapse of the growth cone, depending on the context and the specific Eph/ephrin pair involved.

Mutations in EphA1 have been associated with various diseases, including cancer, neurodevelopmental disorders, and cardiovascular disease.

Ephrin-B3 is a type of protein that belongs to the ephrin family and is involved in cell signaling, particularly during the development and functioning of the nervous system. It is a transmembrane protein, which means it spans the membrane of the cell and has a domain outside the cell and a domain inside the cell.

Ephrin-B3 interacts with Eph receptors on neighboring cells to initiate bidirectional signaling, which means that both the cells that express ephrin-B3 and the cells that express the Eph receptor are affected by this interaction. This signaling is important for various processes such as axon guidance, cell migration, and tissue boundaries formation during development. In addition, ephrin-B3 has been implicated in the regulation of synaptic plasticity and vascular remodeling in adults.

Mutations in the gene that encodes ephrin-B3 have been associated with certain neurological disorders, such as intellectual disability and epilepsy.

EphB4 is a type of receptor tyrosine kinase (RTK) that belongs to the Eph receptor family. These receptors are involved in cell-cell communication during development and tissue homeostasis. Specifically, EphB4 is a membrane-bound protein that interacts with its ligand, ephrin-B2, which is also a transmembrane protein, to mediate bidirectional signaling between neighboring cells.

The binding of ephrin-B2 to EphB4 triggers a variety of intracellular signaling events that regulate various cellular processes, including cell migration, adhesion, and repulsion. In the context of the cardiovascular system, EphB4 plays important roles in vascular development, angiogenesis, and arterial-venous specification.

Mutations or dysregulation of EphB4 have been implicated in various pathological conditions, such as cancer, atherosclerosis, and neurological disorders. Therefore, understanding the function and regulation of EphB4 has important implications for the development of novel therapeutic strategies for these diseases.

Ephrin-A3 is a type of protein that belongs to the ephrin family. Ephrins are membrane-bound proteins that play crucial roles in various biological processes, including cell signaling and communication during development. Specifically, Ephrin-A3 binds to Eph receptors, which are tyrosine kinase receptors found on the surface of neighboring cells. This binding leads to bidirectional signals that regulate cell adhesion, repulsion, and migration, thereby helping to establish proper tissue and organ architecture during development. Additionally, Ephrin-A3 has been implicated in various physiological and pathological processes, such as angiogenesis, neurogenesis, and cancer.

EphA3 is a type of receptor tyrosine kinase (RTK) that belongs to the Eph family of receptors. It is a transmembrane protein involved in cell-cell communication and signal transduction. The EphA3 receptor specifically binds to ephrin-A5, its ligand, leading to various intracellular signaling events that regulate cell behavior, including cell migration, adhesion, and differentiation.

EphA3 is widely expressed in various tissues, including the nervous system, hematopoietic cells, and epithelial cells. In the nervous system, EphA3 plays a crucial role in axon guidance and neuronal positioning during development. In hematopoietic cells, it has been implicated in the regulation of immune cell function and the development of certain types of leukemia.

Mutations or aberrant expression of EphA3 have been associated with several diseases, including cancer, making it a potential target for therapeutic intervention.

EphB2 is a type of receptor tyrosine kinase (RTK) that belongs to the Eph family of receptors. These receptors are involved in bidirectional communication between cells and are important in the development and function of the nervous system. Specifically, EphB2 receptors are expressed on the surface of certain types of neurons and bind to ephrin-B ligands on nearby cells. This binding triggers a cascade of intracellular signaling events that can regulate various cellular processes, including cell migration, adhesion, and axon guidance.

EphB2 receptors have also been implicated in the pathology of several diseases, including cancer. For example, abnormal activation of EphB2 has been linked to tumor growth, progression, and metastasis in certain types of cancer. Therefore, EphB2 is an important target for the development of new therapies for cancer and other diseases.

EphA2 is a type of receptor tyrosine kinase (RTK) that belongs to the Eph (Erythropoietin-producing hepatocellular) family of receptors. It is a transmembrane protein found on the surface of many types of cells, including epithelial, endothelial, and cancer cells.

EphA2 receptors play critical roles in various biological processes such as cell growth, survival, migration, and angiogenesis. They interact with their ligands, called ephrins, which are also transmembrane proteins expressed on adjacent cells. The interaction between EphA2 and ephrins triggers bidirectional signaling that can regulate the adhesion, repulsion, or movement of cells in response to contact with other cells.

In cancer biology, EphA2 receptors have been implicated in tumor progression and metastasis. Overexpression of EphA2 has been observed in various types of human cancers, including breast, lung, prostate, ovarian, and colon cancer. High levels of EphA2 are often associated with poor clinical outcomes, making it an attractive therapeutic target for cancer treatment.

EphA5 is a type of receptor tyrosine kinase that belongs to the Eph receptor family. Eph receptors are the largest subfamily of receptor tyrosine kinases and play critical roles in various biological processes, including cell migration, axon guidance, and tissue boundary formation during embryonic development.

EphA5 receptor specifically binds to ephrin-A5 ligand, which is a member of the ephrin family of membrane-bound proteins. The binding of ephrin-A5 to EphA5 triggers bidirectional signaling, meaning that both the receptor and the ligand can transmit signals into their respective cells. This interaction leads to various cellular responses, such as changes in cytoskeletal organization, cell adhesion, and intracellular signaling pathways.

EphA5 has been implicated in several physiological and pathological processes, including neural development, vascular remodeling, tumor angiogenesis, and cancer metastasis. Mutations in the EPHA5 gene have been associated with various human diseases, such as intellectual disability, epilepsy, and congenital heart defects.

EphA7 is a type of receptor that belongs to the EPH receptor tyrosine kinase family. These receptors are involved in intracellular signaling and play crucial roles in various biological processes, including cell growth, differentiation, and migration.

EphA7 receptors are specifically activated by ephrin-A ligands, which are membrane-bound proteins expressed on adjacent cells. When an ephrin-A ligand binds to an EphA7 receptor, it triggers a cascade of intracellular signaling events that can affect various cellular functions.

EphA7 receptors have been implicated in several physiological and pathological processes, including nervous system development, angiogenesis, and cancer. In the nervous system, EphA7 receptors help to establish connections between neurons and guide their migration during development. In cancer, abnormal expression or activation of EphA7 receptors has been linked to tumor growth, progression, and metastasis.

It's worth noting that while I strive to provide accurate and up-to-date information, medical definitions can be complex and nuanced. Therefore, it may be helpful to consult authoritative medical resources or speak with a healthcare professional for more detailed information on this topic.

EphB3 is a type of receptor tyrosine kinase that belongs to the Eph family of receptors. It is a transmembrane protein that plays a crucial role in cell signaling and communication, particularly during embryonic development and tissue organization. The EphB3 receptor binds to ephrin-B ligands, which are also transmembrane proteins expressed on neighboring cells.

The binding of ephrin-B to EphB3 initiates a bidirectional signaling process that regulates various cellular processes such as cell adhesion, migration, and repulsion. This interaction is important for the formation of boundaries between different tissues, axon guidance, and synaptic plasticity in the nervous system.

Mutations in the EphB3 gene have been associated with several human diseases, including cancer, immune disorders, and neurological conditions. Therefore, understanding the function and regulation of EphB3 receptors is essential for developing novel therapeutic strategies to treat these diseases.

EphB1 is a type of receptor tyrosine kinase (RTK) that belongs to the Eph family of receptors. It is a single-pass transmembrane protein that contains an extracellular domain with a binding site for its ligand, ephrin-Bs, and an intracellular domain with tyrosine kinase activity.

EphB1 receptors are primarily expressed in the nervous system, where they play important roles in various developmental processes, including axon guidance, neuronal migration, and synaptic plasticity. They also have been implicated in tumorigenesis and cancer progression, as well as in the regulation of immune responses.

The binding of ephrin-Bs to EphB1 receptors triggers a variety of intracellular signaling pathways that can lead to both forward and reverse signaling. Forward signaling occurs when the activated EphB1 receptor phosphorylates downstream effector proteins, leading to changes in cell behavior such as repulsion or adhesion. Reverse signaling occurs when ephrin-Bs, which are also transmembrane proteins, activate their own intracellular signaling pathways upon binding to EphB1 receptors.

Overall, the EphB1 receptor is a crucial component of the Eph/ephrin signaling system that plays important roles in various biological processes and has potential implications for disease treatment and diagnosis.

Signal transduction is the process by which a cell converts an extracellular signal, such as a hormone or neurotransmitter, into an intracellular response. This involves a series of molecular events that transmit the signal from the cell surface to the interior of the cell, ultimately resulting in changes in gene expression, protein activity, or metabolism.

The process typically begins with the binding of the extracellular signal to a receptor located on the cell membrane. This binding event activates the receptor, which then triggers a cascade of intracellular signaling molecules, such as second messengers, protein kinases, and ion channels. These molecules amplify and propagate the signal, ultimately leading to the activation or inhibition of specific cellular responses.

Signal transduction pathways are highly regulated and can be modulated by various factors, including other signaling molecules, post-translational modifications, and feedback mechanisms. Dysregulation of these pathways has been implicated in a variety of diseases, including cancer, diabetes, and neurological disorders.

The anterior capsule of the lens is a thin, transparent membrane that forms the front part of the capsule surrounding the crystalline lens in the eye. It is an important structure in cataract surgery where it is removed to gain access to and remove the cloudy lens material. The posterior capsule, which is located behind the lens, may also become opacified following cataract surgery, causing a secondary type of cataract known as a "posterior capsular opacity."

Protein Tyrosine Phosphatase, Non-Receptor Type 13 (PTPN13), also known as PTP Delta or PTPD, is a protein tyrosine phosphatase enzyme that plays a crucial role in regulating various cellular processes, including cell growth, differentiation, and migration. It is a non-receptor type phosphatase, meaning it does not have a transmembrane domain and is localized in the cytoplasm.

PTPN13 contains several functional domains, including a catalytic domain that dephosphorylates tyrosine residues on target proteins, a protein-protein interaction domain, and a focal adhesion targeting (FAT) domain that localizes the enzyme to focal adhesions, which are sites of cell-matrix contact.

PTPN13 has been shown to interact with and dephosphorylate several signaling molecules, including receptor tyrosine kinases, adaptor proteins, and small GTPases, thereby regulating various downstream signaling pathways involved in cell survival, proliferation, and migration. Dysregulation of PTPN13 has been implicated in the development and progression of several diseases, including cancer, cardiovascular disease, and neurological disorders.

EphB6 is not a traditional "receptor" in the sense of a protein that binds to a signaling molecule and triggers a cellular response. Instead, EphB6 is a member of the Eph receptor tyrosine kinase family, which are involved in intracellular signaling pathways.

EphB6 is unique among the Eph receptors because it lacks a functional kinase domain and is therefore considered to be a "non-kinase" member of the family. Instead, EphB6 forms complexes with other Eph receptors and modulates their signaling activity.

EphB6 has been shown to interact with other Eph receptors, such as EphB2 and EphB3, and regulate their downstream signaling pathways. It is involved in various cellular processes, including cell adhesion, migration, and differentiation. Dysregulation of EphB6 has been implicated in several diseases, including cancer, where it can act as a tumor suppressor or promote tumor progression depending on the context.

In summary, while EphB6 is not a traditional receptor that binds to signaling molecules and triggers cellular responses, it is a member of the Eph receptor tyrosine kinase family that modulates the signaling activity of other Eph receptors and plays important roles in various cellular processes.

EphA8 is a type of receptor tyrosine kinase (RTK) that belongs to the Eph receptor subfamily, which is the largest subfamily of RTKs. These receptors are involved in various biological processes, including cell-cell communication, cell migration, and tissue boundary formation during development.

EphA8 receptors specifically bind to ephrin-A ligands, which are membrane-bound proteins expressed on adjacent cells. The binding of ephrin-A to EphA8 initiates a bidirectional signaling process that affects both the receptor-expressing and ligand-expressing cells. This interaction can result in either attraction or repulsion between the cells, depending on the context and the specific ephrin-A/EphA8 pair involved.

In summary, EphA8 is a cell surface receptor that binds to ephrin-A ligands to mediate cell-cell communication and regulate various developmental processes.

Growth cones are specialized structures found at the tips of growing neurites (axons and dendrites) during the development and regeneration of the nervous system. They were first described by Santiago Ramón y Cajal in the late 19th century. Growth cones play a crucial role in the process of neurogenesis, guiding the extension and pathfinding of axons to their appropriate targets through a dynamic interplay with environmental cues. These cues include various guidance molecules, such as netrins, semaphorins, ephrins, and slits, which bind to receptors on the growth cone membrane and trigger intracellular signaling cascades that ultimately determine the direction of axonal outgrowth.

Morphologically, a growth cone consists of three main parts: the central domain (or "C-domain"), the peripheral domain (or "P-domain"), and the transition zone connecting them. The C-domain contains microtubules and neurofilaments, which provide structural support and transport materials to the growing neurite. The P-domain is rich in actin filaments and contains numerous membrane protrusions called filopodia and lamellipodia, which explore the environment for guidance cues and facilitate motility.

The dynamic behavior of growth cones allows them to navigate complex environments, make decisions at choice points, and ultimately form precise neural circuits during development. Understanding the mechanisms that regulate growth cone function is essential for developing strategies to promote neural repair and regeneration in various neurological disorders and injuries.

A ligand, in the context of biochemistry and medicine, is a molecule that binds to a specific site on a protein or a larger biomolecule, such as an enzyme or a receptor. This binding interaction can modify the function or activity of the target protein, either activating it or inhibiting it. Ligands can be small molecules, like hormones or neurotransmitters, or larger structures, like antibodies. The study of ligand-protein interactions is crucial for understanding cellular processes and developing drugs, as many therapeutic compounds function by binding to specific targets within the body.

P120 GTPase activating protein (GAP) is not a commonly used medical term, and it may be more accurate to describe it as a term from cell biology. However, I can still provide you with some information about this protein.

P120 GTPase activating protein is a type of protein that functions as a negative regulator of RhoA, Rac, and Cdc42, which are members of the Rho family of GTPases. These GTPases play crucial roles in regulating various cellular processes such as cell adhesion, migration, proliferation, and differentiation.

P120 GAP contains a conserved catalytic domain that promotes the hydrolysis of GTP to GDP, thereby turning off RhoA, Rac, and Cdc42 signaling pathways. P120 GAP has been implicated in various cellular processes, including the regulation of cadherin-based adhesion complexes, cell migration, and tumor suppression.

Mutations in the p120 GAP gene have been associated with several types of cancer, including colon, lung, and breast cancer, suggesting that this protein may play a critical role in preventing tumor development and progression.

An axon is a long, slender extension of a neuron (a type of nerve cell) that conducts electrical impulses (nerve impulses) away from the cell body to target cells, such as other neurons or muscle cells. Axons can vary in length from a few micrometers to over a meter long and are typically surrounded by a myelin sheath, which helps to insulate and protect the axon and allows for faster transmission of nerve impulses.

Axons play a critical role in the functioning of the nervous system, as they provide the means by which neurons communicate with one another and with other cells in the body. Damage to axons can result in serious neurological problems, such as those seen in spinal cord injuries or neurodegenerative diseases like multiple sclerosis.

Morphogenesis is a term used in developmental biology and refers to the process by which cells give rise to tissues and organs with specific shapes, structures, and patterns during embryonic development. This process involves complex interactions between genes, cells, and the extracellular environment that result in the coordinated movement and differentiation of cells into specialized functional units.

Morphogenesis is a dynamic and highly regulated process that involves several mechanisms, including cell proliferation, death, migration, adhesion, and differentiation. These processes are controlled by genetic programs and signaling pathways that respond to environmental cues and regulate the behavior of individual cells within a developing tissue or organ.

The study of morphogenesis is important for understanding how complex biological structures form during development and how these processes can go awry in disease states such as cancer, birth defects, and degenerative disorders.

Receptor Protein-Tyrosine Kinases (RTKs) are a type of transmembrane receptors found on the cell surface that play a crucial role in signal transduction and regulation of various cellular processes, including cell growth, differentiation, metabolism, and survival. They are called "tyrosine kinases" because they possess an intrinsic enzymatic activity that catalyzes the transfer of a phosphate group from ATP to tyrosine residues on target proteins, thereby modulating their function.

RTKs are composed of three main domains: an extracellular domain that binds to specific ligands (growth factors, hormones, or cytokines), a transmembrane domain that spans the cell membrane, and an intracellular domain with tyrosine kinase activity. Upon ligand binding, RTKs undergo conformational changes that lead to their dimerization or oligomerization, which in turn activates their tyrosine kinase activity. Activated RTKs then phosphorylate specific tyrosine residues on downstream signaling proteins, initiating a cascade of intracellular signaling events that ultimately result in the appropriate cellular response.

Dysregulation of RTK signaling has been implicated in various human diseases, including cancer, diabetes, and developmental disorders. As such, RTKs are important targets for therapeutic intervention in these conditions.

Developmental gene expression regulation refers to the processes that control the activation or repression of specific genes during embryonic and fetal development. These regulatory mechanisms ensure that genes are expressed at the right time, in the right cells, and at appropriate levels to guide proper growth, differentiation, and morphogenesis of an organism.

Developmental gene expression regulation is a complex and dynamic process involving various molecular players, such as transcription factors, chromatin modifiers, non-coding RNAs, and signaling molecules. These regulators can interact with cis-regulatory elements, like enhancers and promoters, to fine-tune the spatiotemporal patterns of gene expression during development.

Dysregulation of developmental gene expression can lead to various congenital disorders and developmental abnormalities. Therefore, understanding the principles and mechanisms governing developmental gene expression regulation is crucial for uncovering the etiology of developmental diseases and devising potential therapeutic strategies.

Embryonic structures refer to the various parts and components that develop during the embryonic stage of prenatal development, which occurs from fertilization to the end of the 8th week of gestation. These structures include the primitive streak, notochord, neural tube, heart, somites, and limb buds, among others.

During this stage, the embryo undergoes rapid cell division, differentiation, and organization to form these structures, which will eventually develop into the various organs and systems of the human body. The embryonic structures are formed through a complex process of gene expression, signaling pathways, and interactions between cells and tissues.

Understanding the development of embryonic structures is crucial for understanding normal human development, as well as for identifying abnormalities or defects that may occur during this critical period. This knowledge can also inform medical interventions and treatments to address developmental issues and improve health outcomes for individuals throughout their lives.

Membrane proteins are a type of protein that are embedded in the lipid bilayer of biological membranes, such as the plasma membrane of cells or the inner membrane of mitochondria. These proteins play crucial roles in various cellular processes, including:

1. Cell-cell recognition and signaling
2. Transport of molecules across the membrane (selective permeability)
3. Enzymatic reactions at the membrane surface
4. Energy transduction and conversion
5. Mechanosensation and signal transduction

Membrane proteins can be classified into two main categories: integral membrane proteins, which are permanently associated with the lipid bilayer, and peripheral membrane proteins, which are temporarily or loosely attached to the membrane surface. Integral membrane proteins can further be divided into three subcategories based on their topology:

1. Transmembrane proteins, which span the entire width of the lipid bilayer with one or more alpha-helices or beta-barrels.
2. Lipid-anchored proteins, which are covalently attached to lipids in the membrane via a glycosylphosphatidylinositol (GPI) anchor or other lipid modifications.
3. Monotopic proteins, which are partially embedded in the membrane and have one or more domains exposed to either side of the bilayer.

Membrane proteins are essential for maintaining cellular homeostasis and are targets for various therapeutic interventions, including drug development and gene therapy. However, their structural complexity and hydrophobicity make them challenging to study using traditional biochemical methods, requiring specialized techniques such as X-ray crystallography, nuclear magnetic resonance (NMR) spectroscopy, and single-particle cryo-electron microscopy (cryo-EM).

"Body patterning" is a general term that refers to the process of forming and organizing various tissues and structures into specific patterns during embryonic development. This complex process involves a variety of molecular mechanisms, including gene expression, cell signaling, and cell-cell interactions. It results in the creation of distinct body regions, such as the head, trunk, and limbs, as well as the organization of internal organs and systems.

In medical terminology, "body patterning" may refer to specific developmental processes or abnormalities related to embryonic development. For example, in genetic disorders such as Poland syndrome or Holt-Oram syndrome, mutations in certain genes can lead to abnormal body patterning, resulting in the absence or underdevelopment of certain muscles, bones, or other structures.

It's important to note that "body patterning" is not a formal medical term with a specific definition, but rather a general concept used in developmental biology and genetics.

Cell movement, also known as cell motility, refers to the ability of cells to move independently and change their location within tissue or inside the body. This process is essential for various biological functions, including embryonic development, wound healing, immune responses, and cancer metastasis.

There are several types of cell movement, including:

1. **Crawling or mesenchymal migration:** Cells move by extending and retracting protrusions called pseudopodia or filopodia, which contain actin filaments. This type of movement is common in fibroblasts, immune cells, and cancer cells during tissue invasion and metastasis.
2. **Amoeboid migration:** Cells move by changing their shape and squeezing through tight spaces without forming protrusions. This type of movement is often observed in white blood cells (leukocytes) as they migrate through the body to fight infections.
3. **Pseudopodial extension:** Cells extend pseudopodia, which are temporary cytoplasmic projections containing actin filaments. These protrusions help the cell explore its environment and move forward.
4. **Bacterial flagellar motion:** Bacteria use a whip-like structure called a flagellum to propel themselves through their environment. The rotation of the flagellum is driven by a molecular motor in the bacterial cell membrane.
5. **Ciliary and ependymal movement:** Ciliated cells, such as those lining the respiratory tract and fallopian tubes, have hair-like structures called cilia that beat in coordinated waves to move fluids or mucus across the cell surface.

Cell movement is regulated by a complex interplay of signaling pathways, cytoskeletal rearrangements, and adhesion molecules, which enable cells to respond to environmental cues and navigate through tissues.

The telencephalon is the most anterior (front) region of the embryonic brain, which eventually develops into the largest portion of the adult human brain, including the cerebral cortex, basal ganglia, and olfactory bulbs. It is derived from the prosencephalon (forebrain) during embryonic development and is responsible for higher cognitive functions such as thinking, perception, and language. The telencephalon can be further divided into two hemispheres, each containing regions associated with different functions.

Devazepide is not a medical term, but it is a pharmaceutical compound. It is a selective and competitive antagonist of the benzodiazepine site on GABA(A) receptors. This means that devazepide blocks the effects of benzodiazepines by binding to the same site on the GABA(A) receptor without activating it.

Devazepide has been studied in research settings as a potential treatment for alcohol use disorder and anxiety disorders, but it is not currently approved for medical use in any country.

Therefore, there is no official medical definition for 'Devazepide'.

Quinolinium compounds are a class of organic compounds that contain a quaternary ammonium cation with a quinolinium core. Quinoline is a heterocyclic aromatic organic compound similar to benzene and pyridine, containing two nitrogen atoms at positions 1 and 2 of the six-member ring. When one of the hydrogen atoms in the quinoline is replaced by a positively charged group (such as a methyl or ethyl group), it forms a quaternary ammonium salt, known as a quinolinium compound.

Quinolinium compounds are often used as antimicrobial agents, particularly against gram-positive bacteria and some fungi. They can also be used as building blocks in organic synthesis, catalysts, and dyes. Some examples of quinolinium compounds include quinoline yellow, a food coloring agent, and chloroquine and hydroxychloroquine, drugs used to treat malaria and certain autoimmune diseases.

Nipah virus (NiV) is a zoonotic virus (it is transmitted from animals to humans) that causes severe illness in both humans and animals. It was first identified during an outbreak of disease in pigs and people in Malaysia and Singapore in 1998-1999.

The natural host of the virus are fruit bats of the Pteropodidae Family, Pteropus genus. Transmission to humans may occur through direct contact with infected bats or consumption of date palm sap contaminated by excretions or secretions from infected bats. Human-to-human transmission is also possible through close contact with people's secretions and excretions.

Infection with NiV can lead to a range of clinical presentations, from asymptomatic infection to acute respiratory illness and severe encephalitis (inflammation of the brain). The case fatality rate is estimated to be about 40-75% in humans. There is no vaccine available for either humans or animals. Prevention strategies include avoiding consumption of raw date palm sap, wearing protective clothing while handling infected animals or their contaminated materials, and practicing good hygiene.

The rhombencephalon is a term used in the field of neuroanatomy, which refers to the most posterior region of the developing brain during embryonic development. It is also known as the hindbrain and it gives rise to several important structures in the adult brain.

More specifically, the rhombencephalon can be further divided into two main parts: the metencephalon and the myelencephalon. The metencephalon eventually develops into the pons and cerebellum, while the myelencephalon becomes the medulla oblongata.

The rhombencephalon plays a crucial role in several critical functions of the nervous system, including regulating heart rate and respiration, maintaining balance and posture, and coordinating motor movements. Defects or abnormalities in the development of the rhombencephalon can lead to various neurological disorders, such as cerebellar hypoplasia, Chiari malformation, and certain forms of brainstem tumors.

'Ciona intestinalis' is a species of tunicate, also known as sea squirts. They are marine invertebrate animals that are characterized by their sac-like bodies and filter-feeding habits. Tunicates are members of the phylum Chordata, which includes all animals with dorsal, hollow nerve cords – a category that also contains vertebrates (animals with backbones).

'Ciona intestinalis' is often used as a model organism in biological research due to its simple anatomy and relatively small genome. It has been studied in various fields such as developmental biology, evolution, and biomedical research. The species is native to the waters of the North Atlantic Ocean but has been introduced to many other regions around the world.

Reverse Transcriptase Polymerase Chain Reaction (RT-PCR) is a laboratory technique used in molecular biology to amplify and detect specific DNA sequences. This technique is particularly useful for the detection and quantification of RNA viruses, as well as for the analysis of gene expression.

The process involves two main steps: reverse transcription and polymerase chain reaction (PCR). In the first step, reverse transcriptase enzyme is used to convert RNA into complementary DNA (cDNA) by reading the template provided by the RNA molecule. This cDNA then serves as a template for the PCR amplification step.

In the second step, the PCR reaction uses two primers that flank the target DNA sequence and a thermostable polymerase enzyme to repeatedly copy the targeted cDNA sequence. The reaction mixture is heated and cooled in cycles, allowing the primers to anneal to the template, and the polymerase to extend the new strand. This results in exponential amplification of the target DNA sequence, making it possible to detect even small amounts of RNA or cDNA.

RT-PCR is a sensitive and specific technique that has many applications in medical research and diagnostics, including the detection of viruses such as HIV, hepatitis C virus, and SARS-CoV-2 (the virus that causes COVID-19). It can also be used to study gene expression, identify genetic mutations, and diagnose genetic disorders.

In situ hybridization (ISH) is a molecular biology technique used to detect and localize specific nucleic acid sequences, such as DNA or RNA, within cells or tissues. This technique involves the use of a labeled probe that is complementary to the target nucleic acid sequence. The probe can be labeled with various types of markers, including radioisotopes, fluorescent dyes, or enzymes.

During the ISH procedure, the labeled probe is hybridized to the target nucleic acid sequence in situ, meaning that the hybridization occurs within the intact cells or tissues. After washing away unbound probe, the location of the labeled probe can be visualized using various methods depending on the type of label used.

In situ hybridization has a wide range of applications in both research and diagnostic settings, including the detection of gene expression patterns, identification of viral infections, and diagnosis of genetic disorders.

Cell adhesion refers to the binding of cells to extracellular matrices or to other cells, a process that is fundamental to the development, function, and maintenance of multicellular organisms. Cell adhesion is mediated by various cell surface receptors, such as integrins, cadherins, and immunoglobulin-like cell adhesion molecules (Ig-CAMs), which interact with specific ligands in the extracellular environment. These interactions lead to the formation of specialized junctions, such as tight junctions, adherens junctions, and desmosomes, that help to maintain tissue architecture and regulate various cellular processes, including proliferation, differentiation, migration, and survival. Disruptions in cell adhesion can contribute to a variety of diseases, including cancer, inflammation, and degenerative disorders.

Somites are transient, segmentally repeated embryonic structures that form along the anterior-posterior body axis during vertebrate development. They are derived from the paraxial mesoderm and give rise to various tissues, including the sclerotome (which forms the vertebrae and ribs), myotome (which forms the skeletal muscles of the back and limbs), and dermatome (which forms the dermis of the skin).

Each somite is a block-like structure that is arranged in a repeating pattern along the notochord, which is a flexible rod-like structure that provides mechanical support to the developing embryo. The formation of somites is a critical step in the development of the vertebrate body plan, as they help to establish the segmental organization of the musculoskeletal system and contribute to the formation of other important structures such as the dermis and the circulatory system.

The process of somitogenesis, or the formation of somites, is a highly regulated and coordinated event that involves the interaction of various signaling molecules and genetic pathways. Defects in somite formation can lead to a range of developmental abnormalities, including spinal deformities, muscle weakness, and skin defects.

A nonmammalian embryo refers to the developing organism in animals other than mammals, from the fertilized egg (zygote) stage until hatching or birth. In nonmammalian species, the developmental stages and terminology differ from those used in mammals. The term "embryo" is generally applied to the developing organism up until a specific stage of development that is characterized by the formation of major organs and structures. After this point, the developing organism is referred to as a "larva," "juvenile," or other species-specific terminology.

The study of nonmammalian embryos has played an important role in our understanding of developmental biology and evolutionary developmental biology (evo-devo). By comparing the developmental processes across different animal groups, researchers can gain insights into the evolutionary origins and diversification of body plans and structures. Additionally, nonmammalian embryos are often used as model systems for studying basic biological processes, such as cell division, gene regulation, and pattern formation.

The nervous system is a complex, highly organized network of specialized cells called neurons and glial cells that communicate with each other via electrical and chemical signals to coordinate various functions and activities in the body. It consists of two main parts: the central nervous system (CNS), including the brain and spinal cord, and the peripheral nervous system (PNS), which includes all the nerves and ganglia outside the CNS.

The primary function of the nervous system is to receive, process, and integrate information from both internal and external environments and then respond by generating appropriate motor outputs or behaviors. This involves sensing various stimuli through specialized receptors, transmitting this information through afferent neurons to the CNS for processing, integrating this information with other inputs and memories, making decisions based on this processed information, and finally executing responses through efferent neurons that control effector organs such as muscles and glands.

The nervous system can be further divided into subsystems based on their functions, including the somatic nervous system, which controls voluntary movements and reflexes; the autonomic nervous system, which regulates involuntary physiological processes like heart rate, digestion, and respiration; and the enteric nervous system, which is a specialized subset of the autonomic nervous system that controls gut functions. Overall, the nervous system plays a critical role in maintaining homeostasis, regulating behavior, and enabling cognition and consciousness.

A chick embryo refers to the developing organism that arises from a fertilized chicken egg. It is often used as a model system in biological research, particularly during the stages of development when many of its organs and systems are forming and can be easily observed and manipulated. The study of chick embryos has contributed significantly to our understanding of various aspects of developmental biology, including gastrulation, neurulation, organogenesis, and pattern formation. Researchers may use various techniques to observe and manipulate the chick embryo, such as surgical alterations, cell labeling, and exposure to drugs or other agents.

Transgenic mice are genetically modified rodents that have incorporated foreign DNA (exogenous DNA) into their own genome. This is typically done through the use of recombinant DNA technology, where a specific gene or genetic sequence of interest is isolated and then introduced into the mouse embryo. The resulting transgenic mice can then express the protein encoded by the foreign gene, allowing researchers to study its function in a living organism.

The process of creating transgenic mice usually involves microinjecting the exogenous DNA into the pronucleus of a fertilized egg, which is then implanted into a surrogate mother. The offspring that result from this procedure are screened for the presence of the foreign DNA, and those that carry the desired genetic modification are used to establish a transgenic mouse line.

Transgenic mice have been widely used in biomedical research to model human diseases, study gene function, and test new therapies. They provide a valuable tool for understanding complex biological processes and developing new treatments for a variety of medical conditions.

Osteoblasts are specialized bone-forming cells that are derived from mesenchymal stem cells. They play a crucial role in the process of bone formation and remodeling. Osteoblasts synthesize, secrete, and mineralize the organic matrix of bones, which is mainly composed of type I collagen.

These cells have receptors for various hormones and growth factors that regulate their activity, such as parathyroid hormone, vitamin D, and transforming growth factor-beta. When osteoblasts are not actively producing bone matrix, they can become trapped within the matrix they produce, where they differentiate into osteocytes, which are mature bone cells that play a role in maintaining bone structure and responding to mechanical stress.

Abnormalities in osteoblast function can lead to various bone diseases, such as osteoporosis, osteogenesis imperfecta, and Paget's disease of bone.

Receptor cross-talk, also known as receptor crosstalk or cross-communication, refers to the phenomenon where two or more receptors in a cell interact with each other and modulate their signals in a coordinated manner. This interaction can occur at various levels, such as sharing downstream signaling pathways, physically interacting with each other, or influencing each other's expression or activity.

In the context of G protein-coupled receptors (GPCRs), which are a large family of membrane receptors that play crucial roles in various physiological processes, cross-talk can occur between different GPCRs or between GPCRs and other types of receptors. For example, one GPCR may activate a signaling pathway that inhibits the activity of another GPCR, leading to complex regulatory mechanisms that allow cells to fine-tune their responses to various stimuli.

Receptor cross-talk can have important implications for drug development and therapy, as it can affect the efficacy and safety of drugs that target specific receptors. Understanding the mechanisms of receptor cross-talk can help researchers design more effective and targeted therapies for a wide range of diseases.

"Cells, cultured" is a medical term that refers to cells that have been removed from an organism and grown in controlled laboratory conditions outside of the body. This process is called cell culture and it allows scientists to study cells in a more controlled and accessible environment than they would have inside the body. Cultured cells can be derived from a variety of sources, including tissues, organs, or fluids from humans, animals, or cell lines that have been previously established in the laboratory.

Cell culture involves several steps, including isolation of the cells from the tissue, purification and characterization of the cells, and maintenance of the cells in appropriate growth conditions. The cells are typically grown in specialized media that contain nutrients, growth factors, and other components necessary for their survival and proliferation. Cultured cells can be used for a variety of purposes, including basic research, drug development and testing, and production of biological products such as vaccines and gene therapies.

It is important to note that cultured cells may behave differently than they do in the body, and results obtained from cell culture studies may not always translate directly to human physiology or disease. Therefore, it is essential to validate findings from cell culture experiments using additional models and ultimately in clinical trials involving human subjects.

Immunohistochemistry (IHC) is a technique used in pathology and laboratory medicine to identify specific proteins or antigens in tissue sections. It combines the principles of immunology and histology to detect the presence and location of these target molecules within cells and tissues. This technique utilizes antibodies that are specific to the protein or antigen of interest, which are then tagged with a detection system such as a chromogen or fluorophore. The stained tissue sections can be examined under a microscope, allowing for the visualization and analysis of the distribution and expression patterns of the target molecule in the context of the tissue architecture. Immunohistochemistry is widely used in diagnostic pathology to help identify various diseases, including cancer, infectious diseases, and immune-mediated disorders.

The superior colliculi are a pair of prominent eminences located on the dorsal surface of the midbrain, forming part of the tectum or roof of the midbrain. They play a crucial role in the integration and coordination of visual, auditory, and somatosensory information for the purpose of directing spatial attention and ocular movements. Essentially, they are involved in the reflexive orienting of the head and eyes towards novel or significant stimuli in the environment.

In a more detailed medical definition, the superior colliculi are two rounded, convex mounds of gray matter that are situated on the roof of the midbrain, specifically at the level of the rostral mesencephalic tegmentum. Each superior colliculus has a stratified laminated structure, consisting of several layers that process different types of sensory information and control specific motor outputs.

The superficial layers of the superior colliculi primarily receive and process visual input from the retina, lateral geniculate nucleus, and other visual areas in the brain. These layers are responsible for generating spatial maps of the visual field, which allow for the localization and identification of visual stimuli.

The intermediate and deep layers of the superior colliculi receive and process auditory and somatosensory information from various sources, including the inferior colliculus, medial geniculate nucleus, and ventral posterior nucleus of the thalamus. These layers are involved in the localization and identification of auditory and tactile stimuli, as well as the coordination of head and eye movements towards these stimuli.

The superior colliculi also contain a population of neurons called "motor command neurons" that directly control the muscles responsible for orienting the eyes, head, and body towards novel or significant sensory events. These motor command neurons are activated in response to specific patterns of activity in the sensory layers of the superior colliculus, allowing for the rapid and automatic orientation of attention and gaze towards salient stimuli.

In summary, the superior colliculi are a pair of structures located on the dorsal surface of the midbrain that play a critical role in the integration and coordination of visual, auditory, and somatosensory information for the purpose of orienting attention and gaze towards salient stimuli. They contain sensory layers that generate spatial maps of the environment, as well as motor command neurons that directly control the muscles responsible for orienting the eyes, head, and body.

A zebrafish is a freshwater fish species belonging to the family Cyprinidae and the genus Danio. Its name is derived from its distinctive striped pattern that resembles a zebra's. Zebrafish are often used as model organisms in scientific research, particularly in developmental biology, genetics, and toxicology studies. They have a high fecundity rate, transparent embryos, and a rapid development process, making them an ideal choice for researchers. However, it is important to note that providing a medical definition for zebrafish may not be entirely accurate or relevant since they are primarily used in biological research rather than clinical medicine.

The skull is the bony structure that encloses and protects the brain, the eyes, and the ears. It is composed of two main parts: the cranium, which contains the brain, and the facial bones. The cranium is made up of several fused flat bones, while the facial bones include the upper jaw (maxilla), lower jaw (mandible), cheekbones, nose bones, and eye sockets (orbits).

The skull also provides attachment points for various muscles that control chewing, moving the head, and facial expressions. Additionally, it contains openings for blood vessels, nerves, and the spinal cord to pass through. The skull's primary function is to protect the delicate and vital structures within it from injury and trauma.

Mitogen-Activated Protein Kinase 9 (MAPK9), also known as c-Jun N-terminal kinase 1 (JNK1), is a serine/threonine protein kinase that plays a crucial role in signal transduction pathways involved in various cellular processes, including inflammation, differentiation, apoptosis, and stress response. It is a member of the MAPK family and is activated by dual phosphorylation on threonine and tyrosine residues within its activation loop by upstream MAPK kinases (MKKs). Once activated, MAPK9/JNK1 translocates to the nucleus where it phosphorylates and regulates the activity of various transcription factors, such as c-Jun, ATF2, and Elk-1, thereby modulating gene expression. Its activation is primarily triggered by stress signals, inflammatory cytokines, and mitogens, making it a key player in the integration and interpretation of extracellular signals to regulate cellular responses.

Messenger RNA (mRNA) is a type of RNA (ribonucleic acid) that carries genetic information copied from DNA in the form of a series of three-base code "words," each of which specifies a particular amino acid. This information is used by the cell's machinery to construct proteins, a process known as translation. After being transcribed from DNA, mRNA travels out of the nucleus to the ribosomes in the cytoplasm where protein synthesis occurs. Once the protein has been synthesized, the mRNA may be degraded and recycled. Post-transcriptional modifications can also occur to mRNA, such as alternative splicing and addition of a 5' cap and a poly(A) tail, which can affect its stability, localization, and translation efficiency.

Veins are blood vessels that carry deoxygenated blood from the tissues back to the heart. They have a lower pressure than arteries and contain valves to prevent the backflow of blood. Veins have a thin, flexible wall with a larger lumen compared to arteries, allowing them to accommodate more blood volume. The color of veins is often blue or green due to the absorption characteristics of light and the reduced oxygen content in the blood they carry.

A "knockout" mouse is a genetically engineered mouse in which one or more genes have been deleted or "knocked out" using molecular biology techniques. This allows researchers to study the function of specific genes and their role in various biological processes, as well as potential associations with human diseases. The mice are generated by introducing targeted DNA modifications into embryonic stem cells, which are then used to create a live animal. Knockout mice have been widely used in biomedical research to investigate gene function, disease mechanisms, and potential therapeutic targets.

Protein binding, in the context of medical and biological sciences, refers to the interaction between a protein and another molecule (known as the ligand) that results in a stable complex. This process is often reversible and can be influenced by various factors such as pH, temperature, and concentration of the involved molecules.

In clinical chemistry, protein binding is particularly important when it comes to drugs, as many of them bind to proteins (especially albumin) in the bloodstream. The degree of protein binding can affect a drug's distribution, metabolism, and excretion, which in turn influence its therapeutic effectiveness and potential side effects.

Protein-bound drugs may be less available for interaction with their target tissues, as only the unbound or "free" fraction of the drug is active. Therefore, understanding protein binding can help optimize dosing regimens and minimize adverse reactions.

Phosphorylation is the process of adding a phosphate group (a molecule consisting of one phosphorus atom and four oxygen atoms) to a protein or other organic molecule, which is usually done by enzymes called kinases. This post-translational modification can change the function, localization, or activity of the target molecule, playing a crucial role in various cellular processes such as signal transduction, metabolism, and regulation of gene expression. Phosphorylation is reversible, and the removal of the phosphate group is facilitated by enzymes called phosphatases.

Neurons, also known as nerve cells or neurocytes, are specialized cells that constitute the basic unit of the nervous system. They are responsible for receiving, processing, and transmitting information and signals within the body. Neurons have three main parts: the dendrites, the cell body (soma), and the axon. The dendrites receive signals from other neurons or sensory receptors, while the axon transmits these signals to other neurons, muscles, or glands. The junction between two neurons is called a synapse, where neurotransmitters are released to transmit the signal across the gap (synaptic cleft) to the next neuron. Neurons vary in size, shape, and structure depending on their function and location within the nervous system.

The retina is the innermost, light-sensitive layer of tissue in the eye of many vertebrates and some cephalopods. It receives light that has been focused by the cornea and lens, converts it into neural signals, and sends these to the brain via the optic nerve. The retina contains several types of photoreceptor cells including rods (which handle vision in low light) and cones (which are active in bright light and are capable of color vision).

In medical terms, any pathological changes or diseases affecting the retinal structure and function can lead to visual impairment or blindness. Examples include age-related macular degeneration, diabetic retinopathy, retinal detachment, and retinitis pigmentosa among others.

Retinal Ganglion Cells (RGCs) are a type of neuron located in the innermost layer of the retina, the light-sensitive tissue at the back of the eye. These cells receive visual information from photoreceptors (rods and cones) via intermediate cells called bipolar cells. RGCs then send this visual information through their long axons to form the optic nerve, which transmits the signals to the brain for processing and interpretation as vision.

There are several types of RGCs, each with distinct morphological and functional characteristics. Some RGCs are specialized in detecting specific features of the visual scene, such as motion, contrast, color, or brightness. The diversity of RGCs allows for a rich and complex representation of the visual world in the brain.

Damage to RGCs can lead to various visual impairments, including loss of vision, reduced visual acuity, and altered visual fields. Conditions associated with RGC damage or degeneration include glaucoma, optic neuritis, ischemic optic neuropathy, and some inherited retinal diseases.

The umbilical cord is a flexible, tube-like structure that connects the developing fetus to the placenta in the uterus during pregnancy. It arises from the abdomen of the fetus and transports essential nutrients, oxygen, and blood from the mother's circulation to the growing baby. Additionally, it carries waste products, such as carbon dioxide, from the fetus back to the placenta for elimination. The umbilical cord is primarily composed of two arteries (the umbilical arteries) and one vein (the umbilical vein), surrounded by a protective gelatinous substance called Wharton's jelly, and enclosed within a fibrous outer covering known as the umbilical cord coating. Following birth, the umbilical cord is clamped and cut, leaving behind the stump that eventually dries up and falls off, resulting in the baby's belly button.

Tertiary protein structure refers to the three-dimensional arrangement of all the elements (polypeptide chains) of a single protein molecule. It is the highest level of structural organization and results from interactions between various side chains (R groups) of the amino acids that make up the protein. These interactions, which include hydrogen bonds, ionic bonds, van der Waals forces, and disulfide bridges, give the protein its unique shape and stability, which in turn determines its function. The tertiary structure of a protein can be stabilized by various factors such as temperature, pH, and the presence of certain ions. Any changes in these factors can lead to denaturation, where the protein loses its tertiary structure and thus its function.

C57BL/6 (C57 Black 6) is an inbred strain of laboratory mouse that is widely used in biomedical research. The term "inbred" refers to a strain of animals where matings have been carried out between siblings or other closely related individuals for many generations, resulting in a population that is highly homozygous at most genetic loci.

The C57BL/6 strain was established in 1920 by crossing a female mouse from the dilute brown (DBA) strain with a male mouse from the black strain. The resulting offspring were then interbred for many generations to create the inbred C57BL/6 strain.

C57BL/6 mice are known for their robust health, longevity, and ease of handling, making them a popular choice for researchers. They have been used in a wide range of biomedical research areas, including studies of cancer, immunology, neuroscience, cardiovascular disease, and metabolism.

One of the most notable features of the C57BL/6 strain is its sensitivity to certain genetic modifications, such as the introduction of mutations that lead to obesity or impaired glucose tolerance. This has made it a valuable tool for studying the genetic basis of complex diseases and traits.

Overall, the C57BL/6 inbred mouse strain is an important model organism in biomedical research, providing a valuable resource for understanding the genetic and molecular mechanisms underlying human health and disease.

Cell communication, also known as cell signaling, is the process by which cells exchange and transmit signals between each other and their environment. This complex system allows cells to coordinate their functions and maintain tissue homeostasis. Cell communication can occur through various mechanisms including:

1. Autocrine signaling: When a cell releases a signal that binds to receptors on the same cell, leading to changes in its behavior or function.
2. Paracrine signaling: When a cell releases a signal that binds to receptors on nearby cells, influencing their behavior or function.
3. Endocrine signaling: When a cell releases a hormone into the bloodstream, which then travels to distant target cells and binds to specific receptors, triggering a response.
4. Synaptic signaling: In neurons, communication occurs through the release of neurotransmitters that cross the synapse and bind to receptors on the postsynaptic cell, transmitting electrical or chemical signals.
5. Contact-dependent signaling: When cells physically interact with each other, allowing for the direct exchange of signals and information.

Cell communication is essential for various physiological processes such as growth, development, differentiation, metabolism, immune response, and tissue repair. Dysregulation in cell communication can contribute to diseases, including cancer, diabetes, and neurological disorders.

Biological models, also known as physiological models or organismal models, are simplified representations of biological systems, processes, or mechanisms that are used to understand and explain the underlying principles and relationships. These models can be theoretical (conceptual or mathematical) or physical (such as anatomical models, cell cultures, or animal models). They are widely used in biomedical research to study various phenomena, including disease pathophysiology, drug action, and therapeutic interventions.

Examples of biological models include:

1. Mathematical models: These use mathematical equations and formulas to describe complex biological systems or processes, such as population dynamics, metabolic pathways, or gene regulation networks. They can help predict the behavior of these systems under different conditions and test hypotheses about their underlying mechanisms.
2. Cell cultures: These are collections of cells grown in a controlled environment, typically in a laboratory dish or flask. They can be used to study cellular processes, such as signal transduction, gene expression, or metabolism, and to test the effects of drugs or other treatments on these processes.
3. Animal models: These are living organisms, usually vertebrates like mice, rats, or non-human primates, that are used to study various aspects of human biology and disease. They can provide valuable insights into the pathophysiology of diseases, the mechanisms of drug action, and the safety and efficacy of new therapies.
4. Anatomical models: These are physical representations of biological structures or systems, such as plastic models of organs or tissues, that can be used for educational purposes or to plan surgical procedures. They can also serve as a basis for developing more sophisticated models, such as computer simulations or 3D-printed replicas.

Overall, biological models play a crucial role in advancing our understanding of biology and medicine, helping to identify new targets for therapeutic intervention, develop novel drugs and treatments, and improve human health.

Cell differentiation is the process by which a less specialized cell, or stem cell, becomes a more specialized cell type with specific functions and structures. This process involves changes in gene expression, which are regulated by various intracellular signaling pathways and transcription factors. Differentiation results in the development of distinct cell types that make up tissues and organs in multicellular organisms. It is a crucial aspect of embryonic development, tissue repair, and maintenance of homeostasis in the body.

Gene expression is the process by which the information encoded in a gene is used to synthesize a functional gene product, such as a protein or RNA molecule. This process involves several steps: transcription, RNA processing, and translation. During transcription, the genetic information in DNA is copied into a complementary RNA molecule, known as messenger RNA (mRNA). The mRNA then undergoes RNA processing, which includes adding a cap and tail to the mRNA and splicing out non-coding regions called introns. The resulting mature mRNA is then translated into a protein on ribosomes in the cytoplasm through the process of translation.

The regulation of gene expression is a complex and highly controlled process that allows cells to respond to changes in their environment, such as growth factors, hormones, and stress signals. This regulation can occur at various stages of gene expression, including transcriptional activation or repression, RNA processing, mRNA stability, and translation. Dysregulation of gene expression has been implicated in many diseases, including cancer, genetic disorders, and neurological conditions.

Electroporation is a medical procedure that involves the use of electrical fields to create temporary pores or openings in the cell membrane, allowing for the efficient uptake of molecules, drugs, or genetic material into the cell. This technique can be used for various purposes, including delivering genes in gene therapy, introducing drugs for cancer treatment, or transforming cells in laboratory research. The electrical pulses are carefully controlled to ensure that they are strong enough to create pores in the membrane without causing permanent damage to the cell. After the electrical field is removed, the pores typically close and the cell membrane returns to its normal state.

The neural crest is a transient, multipotent embryonic cell population that originates from the ectoderm (outermost layer) of the developing neural tube (precursor to the central nervous system). These cells undergo an epithelial-to-mesenchymal transition and migrate throughout the embryo, giving rise to a diverse array of cell types and structures.

Neural crest cells differentiate into various tissues, including:

1. Peripheral nervous system (PNS) components: sensory neurons, sympathetic and parasympathetic ganglia, and glial cells (e.g., Schwann cells).
2. Facial bones and cartilage, as well as connective tissue of the skull.
3. Melanocytes, which are pigment-producing cells in the skin.
4. Smooth muscle cells in major blood vessels, heart, gastrointestinal tract, and other organs.
5. Secretory cells in endocrine glands (e.g., chromaffin cells of the adrenal medulla).
6. Parts of the eye, such as the cornea and iris stroma.
7. Dental tissues, including dentin, cementum, and dental pulp.

Due to their wide-ranging contributions to various tissues and organs, neural crest cells play a crucial role in embryonic development and organogenesis. Abnormalities in neural crest cell migration or differentiation can lead to several congenital disorders, such as neurocristopathies.

Real-Time Polymerase Chain Reaction (RT-PCR) is a laboratory technique used in molecular biology to amplify and detect specific DNA sequences in real-time. It is a sensitive and specific method that allows for the quantification of target nucleic acids, such as DNA or RNA, through the use of fluorescent reporter molecules.

The RT-PCR process involves several steps: first, the template DNA is denatured to separate the double-stranded DNA into single strands. Then, primers (short sequences of DNA) specific to the target sequence are added and allowed to anneal to the template DNA. Next, a heat-stable enzyme called Taq polymerase adds nucleotides to the annealed primers, extending them along the template DNA until a new double-stranded DNA molecule is formed.

During each amplification cycle, fluorescent reporter molecules are added that bind specifically to the newly synthesized DNA. As more and more copies of the target sequence are generated, the amount of fluorescence increases in proportion to the number of copies present. This allows for real-time monitoring of the PCR reaction and quantification of the target nucleic acid.

RT-PCR is commonly used in medical diagnostics, research, and forensics to detect and quantify specific DNA or RNA sequences. It has been widely used in the diagnosis of infectious diseases, genetic disorders, and cancer, as well as in the identification of microbial pathogens and the detection of gene expression.

An amino acid sequence is the specific order of amino acids in a protein or peptide molecule, formed by the linking of the amino group (-NH2) of one amino acid to the carboxyl group (-COOH) of another amino acid through a peptide bond. The sequence is determined by the genetic code and is unique to each type of protein or peptide. It plays a crucial role in determining the three-dimensional structure and function of proteins.

Molecular sequence data refers to the specific arrangement of molecules, most commonly nucleotides in DNA or RNA, or amino acids in proteins, that make up a biological macromolecule. This data is generated through laboratory techniques such as sequencing, and provides information about the exact order of the constituent molecules. This data is crucial in various fields of biology, including genetics, evolution, and molecular biology, allowing for comparisons between different organisms, identification of genetic variations, and studies of gene function and regulation.

"Gene knockout techniques" refer to a group of biomedical research methods used in genetics and molecular biology to study the function of specific genes in an organism. These techniques involve introducing a deliberate, controlled genetic modification that results in the inactivation or "knockout" of a particular gene. This is typically achieved through various methods such as homologous recombination, where a modified version of the gene with inserted mutations is introduced into the organism's genome, replacing the original functional gene. The resulting organism, known as a "knockout mouse" or other model organisms, lacks the function of the targeted gene and can be used to study its role in biological processes, disease development, and potential therapeutic interventions.

Osteoclasts are large, multinucleated cells that are primarily responsible for bone resorption, a process in which they break down and dissolve the mineralized matrix of bones. They are derived from monocyte-macrophage precursor cells of hematopoietic origin and play a crucial role in maintaining bone homeostasis by balancing bone formation and bone resorption.

Osteoclasts adhere to the bone surface and create an isolated microenvironment, called the "resorption lacuna," between their cell membrane and the bone surface. Here, they release hydrogen ions into the lacuna through a process called proton pumping, which lowers the pH and dissolves the mineral component of the bone matrix. Additionally, osteoclasts secrete proteolytic enzymes, such as cathepsin K, that degrade the organic components, like collagen, in the bone matrix.

An imbalance in osteoclast activity can lead to various bone diseases, including osteoporosis and Paget's disease, where excessive bone resorption results in weakened and fragile bones.

Up-regulation is a term used in molecular biology and medicine to describe an increase in the expression or activity of a gene, protein, or receptor in response to a stimulus. This can occur through various mechanisms such as increased transcription, translation, or reduced degradation of the molecule. Up-regulation can have important functional consequences, for example, enhancing the sensitivity or response of a cell to a hormone, neurotransmitter, or drug. It is a normal physiological process that can also be induced by disease or pharmacological interventions.

Zebrafish proteins refer to the diverse range of protein molecules that are produced by the organism Danio rerio, commonly known as the zebrafish. These proteins play crucial roles in various biological processes such as growth, development, reproduction, and response to environmental stimuli. They are involved in cellular functions like enzymatic reactions, signal transduction, structural support, and regulation of gene expression.

Zebrafish is a popular model organism in biomedical research due to its genetic similarity with humans, rapid development, and transparent embryos that allow for easy observation of biological processes. As a result, the study of zebrafish proteins has contributed significantly to our understanding of protein function, structure, and interaction in both zebrafish and human systems.

Some examples of zebrafish proteins include:

* Transcription factors that regulate gene expression during development
* Enzymes involved in metabolic pathways
* Structural proteins that provide support to cells and tissues
* Receptors and signaling molecules that mediate communication between cells
* Heat shock proteins that assist in protein folding and protect against stress

The analysis of zebrafish proteins can be performed using various techniques, including biochemical assays, mass spectrometry, protein crystallography, and computational modeling. These methods help researchers to identify, characterize, and understand the functions of individual proteins and their interactions within complex networks.

The umbilical veins are blood vessels in the umbilical cord that carry oxygenated and nutrient-rich blood from the mother to the developing fetus during pregnancy. There are typically two umbilical veins, one of which usually degenerates and becomes obliterated, leaving a single functional vein. This remaining vein is known as the larger umbilical vein or the venous duct. It enters the fetal abdomen through the umbilicus and passes through the liver, where it branches off to form the portal sinus. Ultimately, the blood from the umbilical vein mixes with the blood from the inferior vena cava and is pumped to the heart through the right atrium.

It's important to note that after birth, the umbilical veins are no longer needed and undergo involution, becoming the ligamentum teres in the adult.

Osteogenesis is the process of bone formation or development. It involves the differentiation and maturation of osteoblasts, which are bone-forming cells that synthesize and deposit the organic matrix of bone tissue, composed mainly of type I collagen. This organic matrix later mineralizes to form the inorganic crystalline component of bone, primarily hydroxyapatite.

There are two primary types of osteogenesis: intramembranous and endochondral. Intramembranous osteogenesis occurs directly within connective tissue, where mesenchymal stem cells differentiate into osteoblasts and form bone tissue without an intervening cartilage template. This process is responsible for the formation of flat bones like the skull and clavicles.

Endochondral osteogenesis, on the other hand, involves the initial development of a cartilaginous model or template, which is later replaced by bone tissue. This process forms long bones, such as those in the limbs, and occurs through several stages involving chondrocyte proliferation, hypertrophy, and calcification, followed by invasion of blood vessels and osteoblasts to replace the cartilage with bone tissue.

Abnormalities in osteogenesis can lead to various skeletal disorders and diseases, such as osteogenesis imperfecta (brittle bone disease), achondroplasia (a form of dwarfism), and cleidocranial dysplasia (a disorder affecting skull and collarbone development).

Notch receptors are a type of transmembrane receptor proteins that play crucial roles in cell-cell communication and regulation of various biological processes, including cell fate determination, differentiation, proliferation, and apoptosis. These receptors are highly conserved across species and are essential for normal development and tissue homeostasis.

The Notch signaling pathway is initiated when the extracellular domain of a Notch receptor on one cell interacts with its ligand (such as Delta or Jagged) on an adjacent cell. This interaction triggers a series of proteolytic cleavage events that release the intracellular domain of the Notch receptor, which then translocates to the nucleus and regulates gene expression by interacting with transcription factors like CSL (CBF1/RBP-Jκ/Su(H)/Lag-1).

There are four known Notch receptors in humans (Notch1-4) that share a similar structure, consisting of an extracellular domain containing multiple epidermal growth factor (EGF)-like repeats, a transmembrane domain, and an intracellular domain. Mutations or dysregulation of the Notch signaling pathway have been implicated in various human diseases, including cancer, cardiovascular disorders, and developmental abnormalities.

A cell line that is derived from tumor cells and has been adapted to grow in culture. These cell lines are often used in research to study the characteristics of cancer cells, including their growth patterns, genetic changes, and responses to various treatments. They can be established from many different types of tumors, such as carcinomas, sarcomas, and leukemias. Once established, these cell lines can be grown and maintained indefinitely in the laboratory, allowing researchers to conduct experiments and studies that would not be feasible using primary tumor cells. It is important to note that tumor cell lines may not always accurately represent the behavior of the original tumor, as they can undergo genetic changes during their time in culture.

Physiologic neovascularization is the natural and controlled formation of new blood vessels in the body, which occurs as a part of normal growth and development, as well as in response to tissue repair and wound healing. This process involves the activation of endothelial cells, which line the interior surface of blood vessels, and their migration, proliferation, and tube formation to create new capillaries. Physiologic neovascularization is tightly regulated by a balance of pro-angiogenic and anti-angiogenic factors, ensuring that it occurs only when and where it is needed. It plays crucial roles in various physiological processes, such as embryonic development, tissue regeneration, and wound healing.

'Caenorhabditis elegans' is a species of free-living, transparent nematode (roundworm) that is widely used as a model organism in scientific research, particularly in the fields of biology and genetics. It has a simple anatomy, short lifespan, and fully sequenced genome, making it an ideal subject for studying various biological processes and diseases.

Some notable features of C. elegans include:

* Small size: Adult hermaphrodites are about 1 mm in length.
* Short lifespan: The average lifespan of C. elegans is around 2-3 weeks, although some strains can live up to 4 weeks under laboratory conditions.
* Development: C. elegans has a well-characterized developmental process, with adults developing from eggs in just 3 days at 20°C.
* Transparency: The transparent body of C. elegans allows researchers to observe its internal structures and processes easily.
* Genetics: C. elegans has a fully sequenced genome, which contains approximately 20,000 genes. Many of these genes have human homologs, making it an excellent model for studying human diseases.
* Neurobiology: C. elegans has a simple nervous system, with only 302 neurons in the hermaphrodite and 383 in the male. This simplicity makes it an ideal organism for studying neural development, function, and behavior.

Research using C. elegans has contributed significantly to our understanding of various biological processes, including cell division, apoptosis, aging, learning, and memory. Additionally, studies on C. elegans have led to the discovery of many genes associated with human diseases such as cancer, neurodegenerative disorders, and metabolic conditions.

Glial Fibrillary Acidic Protein (GFAP) is a type of intermediate filament protein that is primarily found in astrocytes, which are a type of star-shaped glial cells in the central nervous system (CNS). These proteins play an essential role in maintaining the structural integrity and stability of astrocytes. They also participate in various cellular processes such as responding to injury, providing support to neurons, and regulating the extracellular environment.

GFAP is often used as a marker for astrocytic activation or reactivity, which can occur in response to CNS injuries, neuroinflammation, or neurodegenerative diseases. Elevated GFAP levels in cerebrospinal fluid (CSF) or blood can indicate astrocyte damage or dysfunction and are associated with several neurological conditions, including traumatic brain injury, stroke, multiple sclerosis, Alzheimer's disease, and Alexander's disease.

Green Fluorescent Protein (GFP) is not a medical term per se, but a scientific term used in the field of molecular biology. GFP is a protein that exhibits bright green fluorescence when exposed to light, particularly blue or ultraviolet light. It was originally discovered in the jellyfish Aequorea victoria.

In medical and biological research, scientists often use recombinant DNA technology to introduce the gene for GFP into other organisms, including bacteria, plants, and animals, including humans. This allows them to track the expression and localization of specific genes or proteins of interest in living cells, tissues, or even whole organisms.

The ability to visualize specific cellular structures or processes in real-time has proven invaluable for a wide range of research areas, from studying the development and function of organs and organ systems to understanding the mechanisms of diseases and the effects of therapeutic interventions.

A cell line is a culture of cells that are grown in a laboratory for use in research. These cells are usually taken from a single cell or group of cells, and they are able to divide and grow continuously in the lab. Cell lines can come from many different sources, including animals, plants, and humans. They are often used in scientific research to study cellular processes, disease mechanisms, and to test new drugs or treatments. Some common types of human cell lines include HeLa cells (which come from a cancer patient named Henrietta Lacks), HEK293 cells (which come from embryonic kidney cells), and HUVEC cells (which come from umbilical vein endothelial cells). It is important to note that cell lines are not the same as primary cells, which are cells that are taken directly from a living organism and have not been grown in the lab.

Sequence homology, amino acid, refers to the similarity in the order of amino acids in a protein or a portion of a protein between two or more species. This similarity can be used to infer evolutionary relationships and functional similarities between proteins. The higher the degree of sequence homology, the more likely it is that the proteins are related and have similar functions. Sequence homology can be determined through various methods such as pairwise alignment or multiple sequence alignment, which compare the sequences and calculate a score based on the number and type of matching amino acids.

Small interfering RNA (siRNA) is a type of short, double-stranded RNA molecule that plays a role in the RNA interference (RNAi) pathway. The RNAi pathway is a natural cellular process that regulates gene expression by targeting and destroying specific messenger RNA (mRNA) molecules, thereby preventing the translation of those mRNAs into proteins.

SiRNAs are typically 20-25 base pairs in length and are generated from longer double-stranded RNA precursors called hairpin RNAs or dsRNAs by an enzyme called Dicer. Once generated, siRNAs associate with a protein complex called the RNA-induced silencing complex (RISC), which uses one strand of the siRNA (the guide strand) to recognize and bind to complementary sequences in the target mRNA. The RISC then cleaves the target mRNA, leading to its degradation and the inhibition of protein synthesis.

SiRNAs have emerged as a powerful tool for studying gene function and have shown promise as therapeutic agents for a variety of diseases, including viral infections, cancer, and genetic disorders. However, their use as therapeutics is still in the early stages of development, and there are challenges associated with delivering siRNAs to specific cells and tissues in the body.

Western blotting is a laboratory technique used in molecular biology to detect and quantify specific proteins in a mixture of many different proteins. This technique is commonly used to confirm the expression of a protein of interest, determine its size, and investigate its post-translational modifications. The name "Western" blotting distinguishes this technique from Southern blotting (for DNA) and Northern blotting (for RNA).

The Western blotting procedure involves several steps:

1. Protein extraction: The sample containing the proteins of interest is first extracted, often by breaking open cells or tissues and using a buffer to extract the proteins.
2. Separation of proteins by electrophoresis: The extracted proteins are then separated based on their size by loading them onto a polyacrylamide gel and running an electric current through the gel (a process called sodium dodecyl sulfate-polyacrylamide gel electrophoresis or SDS-PAGE). This separates the proteins according to their molecular weight, with smaller proteins migrating faster than larger ones.
3. Transfer of proteins to a membrane: After separation, the proteins are transferred from the gel onto a nitrocellulose or polyvinylidene fluoride (PVDF) membrane using an electric current in a process called blotting. This creates a replica of the protein pattern on the gel but now immobilized on the membrane for further analysis.
4. Blocking: The membrane is then blocked with a blocking agent, such as non-fat dry milk or bovine serum albumin (BSA), to prevent non-specific binding of antibodies in subsequent steps.
5. Primary antibody incubation: A primary antibody that specifically recognizes the protein of interest is added and allowed to bind to its target protein on the membrane. This step may be performed at room temperature or 4°C overnight, depending on the antibody's properties.
6. Washing: The membrane is washed with a buffer to remove unbound primary antibodies.
7. Secondary antibody incubation: A secondary antibody that recognizes the primary antibody (often coupled to an enzyme or fluorophore) is added and allowed to bind to the primary antibody. This step may involve using a horseradish peroxidase (HRP)-conjugated or alkaline phosphatase (AP)-conjugated secondary antibody, depending on the detection method used later.
8. Washing: The membrane is washed again to remove unbound secondary antibodies.
9. Detection: A detection reagent is added to visualize the protein of interest by detecting the signal generated from the enzyme-conjugated or fluorophore-conjugated secondary antibody. This can be done using chemiluminescent, colorimetric, or fluorescent methods.
10. Analysis: The resulting image is analyzed to determine the presence and quantity of the protein of interest in the sample.

Western blotting is a powerful technique for identifying and quantifying specific proteins within complex mixtures. It can be used to study protein expression, post-translational modifications, protein-protein interactions, and more. However, it requires careful optimization and validation to ensure accurate and reproducible results.

A mutation is a permanent change in the DNA sequence of an organism's genome. Mutations can occur spontaneously or be caused by environmental factors such as exposure to radiation, chemicals, or viruses. They may have various effects on the organism, ranging from benign to harmful, depending on where they occur and whether they alter the function of essential proteins. In some cases, mutations can increase an individual's susceptibility to certain diseases or disorders, while in others, they may confer a survival advantage. Mutations are the driving force behind evolution, as they introduce new genetic variability into populations, which can then be acted upon by natural selection.

X-ray crystallography is a technique used in structural biology to determine the three-dimensional arrangement of atoms in a crystal lattice. In this method, a beam of X-rays is directed at a crystal and diffracts, or spreads out, into a pattern of spots called reflections. The intensity and angle of each reflection are measured and used to create an electron density map, which reveals the position and type of atoms in the crystal. This information can be used to determine the molecular structure of a compound, including its shape, size, and chemical bonds. X-ray crystallography is a powerful tool for understanding the structure and function of biological macromolecules such as proteins and nucleic acids.

Neoplastic gene expression regulation refers to the processes that control the production of proteins and other molecules from genes in neoplastic cells, or cells that are part of a tumor or cancer. In a normal cell, gene expression is tightly regulated to ensure that the right genes are turned on or off at the right time. However, in cancer cells, this regulation can be disrupted, leading to the overexpression or underexpression of certain genes.

Neoplastic gene expression regulation can be affected by a variety of factors, including genetic mutations, epigenetic changes, and signals from the tumor microenvironment. These changes can lead to the activation of oncogenes (genes that promote cancer growth and development) or the inactivation of tumor suppressor genes (genes that prevent cancer).

Understanding neoplastic gene expression regulation is important for developing new therapies for cancer, as targeting specific genes or pathways involved in this process can help to inhibit cancer growth and progression.

A "mutant strain of mice" in a medical context refers to genetically engineered mice that have specific genetic mutations introduced into their DNA. These mutations can be designed to mimic certain human diseases or conditions, allowing researchers to study the underlying biological mechanisms and test potential therapies in a controlled laboratory setting.

Mutant strains of mice are created through various techniques, including embryonic stem cell manipulation, gene editing technologies such as CRISPR-Cas9, and radiation-induced mutagenesis. These methods allow scientists to introduce specific genetic changes into the mouse genome, resulting in mice that exhibit altered physiological or behavioral traits.

These strains of mice are widely used in biomedical research because their short lifespan, small size, and high reproductive rate make them an ideal model organism for studying human diseases. Additionally, the mouse genome has been well-characterized, and many genetic tools and resources are available to researchers working with these animals.

Examples of mutant strains of mice include those that carry mutations in genes associated with cancer, neurodegenerative disorders, metabolic diseases, and immunological conditions. These mice provide valuable insights into the pathophysiology of human diseases and help advance our understanding of potential therapeutic interventions.

Cell proliferation is the process by which cells increase in number, typically through the process of cell division. In the context of biology and medicine, it refers to the reproduction of cells that makes up living tissue, allowing growth, maintenance, and repair. It involves several stages including the transition from a phase of quiescence (G0 phase) to an active phase (G1 phase), DNA replication in the S phase, and mitosis or M phase, where the cell divides into two daughter cells.

Abnormal or uncontrolled cell proliferation is a characteristic feature of many diseases, including cancer, where deregulated cell cycle control leads to excessive and unregulated growth of cells, forming tumors that can invade surrounding tissues and metastasize to distant sites in the body.

'Gene expression regulation' refers to the processes that control whether, when, and where a particular gene is expressed, meaning the production of a specific protein or functional RNA encoded by that gene. This complex mechanism can be influenced by various factors such as transcription factors, chromatin remodeling, DNA methylation, non-coding RNAs, and post-transcriptional modifications, among others. Proper regulation of gene expression is crucial for normal cellular function, development, and maintaining homeostasis in living organisms. Dysregulation of gene expression can lead to various diseases, including cancer and genetic disorders.

Coculture techniques refer to a type of experimental setup in which two or more different types of cells or organisms are grown and studied together in a shared culture medium. This method allows researchers to examine the interactions between different cell types or species under controlled conditions, and to study how these interactions may influence various biological processes such as growth, gene expression, metabolism, and signal transduction.

Coculture techniques can be used to investigate a wide range of biological phenomena, including the effects of host-microbe interactions on human health and disease, the impact of different cell types on tissue development and homeostasis, and the role of microbial communities in shaping ecosystems. These techniques can also be used to test the efficacy and safety of new drugs or therapies by examining their effects on cells grown in coculture with other relevant cell types.

There are several different ways to establish cocultures, depending on the specific research question and experimental goals. Some common methods include:

1. Mixed cultures: In this approach, two or more cell types are simply mixed together in a culture dish or flask and allowed to grow and interact freely.
2. Cell-layer cultures: Here, one cell type is grown on a porous membrane or other support structure, while the second cell type is grown on top of it, forming a layered coculture.
3. Conditioned media cultures: In this case, one cell type is grown to confluence and its culture medium is collected and then used to grow a second cell type. This allows the second cell type to be exposed to any factors secreted by the first cell type into the medium.
4. Microfluidic cocultures: These involve growing cells in microfabricated channels or chambers, which allow for precise control over the spatial arrangement and flow of nutrients, waste products, and signaling molecules between different cell types.

Overall, coculture techniques provide a powerful tool for studying complex biological systems and gaining insights into the mechanisms that underlie various physiological and pathological processes.

Tumor Necrosis Factor (TNF) Receptor II, also known as TNFRSF1B or CD120b, is a type of receptor that binds to the TNF-alpha cytokine and plays a crucial role in the immune system. It is a transmembrane protein mainly expressed on the surface of various cells including immune cells, fibroblasts, and endothelial cells.

The activation of TNFRII by TNF-alpha leads to the initiation of intracellular signaling pathways that regulate inflammatory responses, cell survival, differentiation, and apoptosis (programmed cell death). Dysregulation of this receptor's function has been implicated in several pathological conditions such as autoimmune diseases, cancer, and neurodegenerative disorders.

TNFRII is a member of the TNF receptor superfamily (TNFRSF) and consists of an extracellular domain containing multiple cysteine-rich motifs that facilitate ligand binding, a transmembrane domain, and an intracellular domain responsible for signal transduction. Upon ligand binding, TNFRII forms complexes with various adaptor proteins to activate downstream signaling cascades, ultimately leading to the activation of nuclear factor-kappa B (NF-κB), mitogen-activated protein kinases (MAPKs), and other signaling molecules.

In summary, Tumor Necrosis Factor Receptor II is a key regulator of immune responses and cell fate decisions, with its dysregulation contributing to various pathological conditions.

The cerebral cortex is the outermost layer of the brain, characterized by its intricate folded structure and wrinkled appearance. It is a region of great importance as it plays a key role in higher cognitive functions such as perception, consciousness, thought, memory, language, and attention. The cerebral cortex is divided into two hemispheres, each containing four lobes: the frontal, parietal, temporal, and occipital lobes. These areas are responsible for different functions, with some regions specializing in sensory processing while others are involved in motor control or associative functions. The cerebral cortex is composed of gray matter, which contains neuronal cell bodies, and is covered by a layer of white matter that consists mainly of myelinated nerve fibers.

Beta-catenin is a protein that plays a crucial role in gene transcription and cell-cell adhesion. It is a key component of the Wnt signaling pathway, which regulates various processes such as cell proliferation, differentiation, and migration during embryonic development and tissue homeostasis in adults.

In the absence of Wnt signals, beta-catenin forms a complex with other proteins, including adenomatous polyposis coli (APC) and axin, which targets it for degradation by the proteasome. When Wnt ligands bind to their receptors, this complex is disrupted, allowing beta-catenin to accumulate in the cytoplasm and translocate to the nucleus. In the nucleus, beta-catenin interacts with T cell factor/lymphoid enhancer-binding factor (TCF/LEF) transcription factors to activate the transcription of target genes involved in cell fate determination, survival, and proliferation.

Mutations in the genes encoding components of the Wnt signaling pathway, including beta-catenin, have been implicated in various human diseases, such as cancer, developmental disorders, and degenerative conditions.

Medical Definition:

Matrix Metalloproteinase 13 (MMP-13), also known as collagenase 3, is an enzyme belonging to the family of Matrix Metalloproteinases. These enzymes are involved in the degradation of extracellular matrix components, playing crucial roles in various physiological and pathological processes such as tissue remodeling, wound healing, and cancer progression.

MMP-13 has a specific affinity for cleaving type II collagen, one of the major structural proteins found in articular cartilage. It is also capable of degrading other extracellular matrix components like proteoglycans, elastin, and gelatin. This enzyme is primarily produced by chondrocytes, synovial fibroblasts, and osteoblasts.

Increased expression and activity of MMP-13 have been implicated in the pathogenesis of several diseases, most notably osteoarthritis (OA) and cancer. In OA, overexpression of MMP-13 leads to excessive degradation of articular cartilage, contributing to joint damage and degeneration. In cancer, MMP-13 facilitates tumor cell invasion and metastasis by breaking down the surrounding extracellular matrix.

Regulation of MMP-13 activity is essential for maintaining tissue homeostasis and preventing disease progression. Various therapeutic strategies aiming to inhibit MMP-13 activity are being explored as potential treatments for osteoarthritis and cancer.

Endothelial cells are the type of cells that line the inner surface of blood vessels, lymphatic vessels, and heart chambers. They play a crucial role in maintaining vascular homeostasis by controlling vasomotor tone, coagulation, platelet activation, and inflammation. Endothelial cells also regulate the transport of molecules between the blood and surrounding tissues, and contribute to the maintenance of the structural integrity of the vasculature. They are flat, elongated cells with a unique morphology that allows them to form a continuous, nonthrombogenic lining inside the vessels. Endothelial cells can be isolated from various tissues and cultured in vitro for research purposes.

Nerve regeneration is the process of regrowth and restoration of functional nerve connections following damage or injury to the nervous system. This complex process involves various cellular and molecular events, such as the activation of support cells called glia, the sprouting of surviving nerve fibers (axons), and the reformation of neural circuits. The goal of nerve regeneration is to enable the restoration of normal sensory, motor, and autonomic functions impaired due to nerve damage or injury.

Recombinant fusion proteins are artificially created biomolecules that combine the functional domains or properties of two or more different proteins into a single protein entity. They are generated through recombinant DNA technology, where the genes encoding the desired protein domains are linked together and expressed as a single, chimeric gene in a host organism, such as bacteria, yeast, or mammalian cells.

The resulting fusion protein retains the functional properties of its individual constituent proteins, allowing for novel applications in research, diagnostics, and therapeutics. For instance, recombinant fusion proteins can be designed to enhance protein stability, solubility, or immunogenicity, making them valuable tools for studying protein-protein interactions, developing targeted therapies, or generating vaccines against infectious diseases or cancer.

Examples of recombinant fusion proteins include:

1. Etaglunatide (ABT-523): A soluble Fc fusion protein that combines the heavy chain fragment crystallizable region (Fc) of an immunoglobulin with the extracellular domain of the human interleukin-6 receptor (IL-6R). This fusion protein functions as a decoy receptor, neutralizing IL-6 and its downstream signaling pathways in rheumatoid arthritis.
2. Etanercept (Enbrel): A soluble TNF receptor p75 Fc fusion protein that binds to tumor necrosis factor-alpha (TNF-α) and inhibits its proinflammatory activity, making it a valuable therapeutic option for treating autoimmune diseases like rheumatoid arthritis, ankylosing spondylitis, and psoriasis.
3. Abatacept (Orencia): A fusion protein consisting of the extracellular domain of cytotoxic T-lymphocyte antigen 4 (CTLA-4) linked to the Fc region of an immunoglobulin, which downregulates T-cell activation and proliferation in autoimmune diseases like rheumatoid arthritis.
4. Belimumab (Benlysta): A monoclonal antibody that targets B-lymphocyte stimulator (BLyS) protein, preventing its interaction with the B-cell surface receptor and inhibiting B-cell activation in systemic lupus erythematosus (SLE).
5. Romiplostim (Nplate): A fusion protein consisting of a thrombopoietin receptor agonist peptide linked to an immunoglobulin Fc region, which stimulates platelet production in patients with chronic immune thrombocytopenia (ITP).
6. Darbepoetin alfa (Aranesp): A hyperglycosylated erythropoiesis-stimulating protein that functions as a longer-acting form of recombinant human erythropoietin, used to treat anemia in patients with chronic kidney disease or cancer.
7. Palivizumab (Synagis): A monoclonal antibody directed against the F protein of respiratory syncytial virus (RSV), which prevents RSV infection and is administered prophylactically to high-risk infants during the RSV season.
8. Ranibizumab (Lucentis): A recombinant humanized monoclonal antibody fragment that binds and inhibits vascular endothelial growth factor A (VEGF-A), used in the treatment of age-related macular degeneration, diabetic retinopathy, and other ocular disorders.
9. Cetuximab (Erbitux): A chimeric monoclonal antibody that binds to epidermal growth factor receptor (EGFR), used in the treatment of colorectal cancer and head and neck squamous cell carcinoma.
10. Adalimumab (Humira): A fully humanized monoclonal antibody that targets tumor necrosis factor-alpha (TNF-α), used in the treatment of various inflammatory diseases, including rheumatoid arthritis, psoriasis, and Crohn's disease.
11. Bevacizumab (Avastin): A recombinant humanized monoclonal antibody that binds to VEGF-A, used in the treatment of various cancers, including colorectal, lung, breast, and kidney cancer.
12. Trastuzumab (Herceptin): A humanized monoclonal antibody that targets HER2/neu receptor, used in the treatment of breast cancer.
13. Rituximab (Rituxan): A chimeric monoclonal antibody that binds to CD20 antigen on B cells, used in the treatment of non-Hodgkin's lymphoma and rheumatoid arthritis.
14. Palivizumab (Synagis): A humanized monoclonal antibody that binds to the F protein of respiratory syncytial virus, used in the prevention of respiratory syncytial virus infection in high-risk infants.
15. Infliximab (Remicade): A chimeric monoclonal antibody that targets TNF-α, used in the treatment of various inflammatory diseases, including Crohn's disease, ulcerative colitis, rheumatoid arthritis, and ankylosing spondylitis.
16. Natalizumab (Tysabri): A humanized monoclonal antibody that binds to α4β1 integrin, used in the treatment of multiple sclerosis and Crohn's disease.
17. Adalimumab (Humira): A fully human monoclonal antibody that targets TNF-α, used in the treatment of various inflammatory diseases, including rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, Crohn's disease, and ulcerative colitis.
18. Golimumab (Simponi): A fully human monoclonal antibody that targets TNF-α, used in the treatment of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, and ulcerative colitis.
19. Certolizumab pegol (Cimzia): A PEGylated Fab' fragment of a humanized monoclonal antibody that targets TNF-α, used in the treatment of rheumatoid arthritis, psoriatic arthritis, ankylosing spondylitis, and Crohn's disease.
20. Ustekinumab (Stelara): A fully human monoclonal antibody that targets IL-12 and IL-23, used in the treatment of psoriasis, psoriatic arthritis, and Crohn's disease.
21. Secukinumab (Cosentyx): A fully human monoclonal antibody that targets IL-17A, used in the treatment of psoriasis, psoriatic arthritis, and ankylosing spondylitis.
22. Ixekizumab (Taltz): A fully human monoclonal antibody that targets IL-17A, used in the treatment of psoriasis and psoriatic arthritis.
23. Brodalumab (Siliq): A fully human monoclonal antibody that targets IL-17 receptor A, used in the treatment of psoriasis.
24. Sarilumab (Kevzara): A fully human monoclonal antibody that targets the IL-6 receptor, used in the treatment of rheumatoid arthritis.
25. Tocilizumab (Actemra): A humanized monoclonal antibody that targets the IL-6 receptor, used in the treatment of rheumatoid arthritis, systemic juvenile idiopathic arthritis, polyarticular juvenile idiopathic arthritis, giant cell arteritis, and chimeric antigen receptor T-cell-induced cytokine release syndrome.
26. Siltuximab (Sylvant): A chimeric monoclonal antibody that targets IL-6, used in the treatment of multicentric Castleman disease.
27. Satralizumab (Enspryng): A humanized monoclonal antibody that targets IL-6 receptor alpha, used in the treatment of neuromyelitis optica spectrum disorder.
28. Sirukumab (Plivensia): A human monoclonal antibody that targets IL-6, used in the treatment

A cell membrane, also known as the plasma membrane, is a thin semi-permeable phospholipid bilayer that surrounds all cells in animals, plants, and microorganisms. It functions as a barrier to control the movement of substances in and out of the cell, allowing necessary molecules such as nutrients, oxygen, and signaling molecules to enter while keeping out harmful substances and waste products. The cell membrane is composed mainly of phospholipids, which have hydrophilic (water-loving) heads and hydrophobic (water-fearing) tails. This unique structure allows the membrane to be flexible and fluid, yet selectively permeable. Additionally, various proteins are embedded in the membrane that serve as channels, pumps, receptors, and enzymes, contributing to the cell's overall functionality and communication with its environment.

Intracellular signaling peptides and proteins are molecules that play a crucial role in transmitting signals within cells, which ultimately lead to changes in cell behavior or function. These signals can originate from outside the cell (extracellular) or within the cell itself. Intracellular signaling molecules include various types of peptides and proteins, such as:

1. G-protein coupled receptors (GPCRs): These are seven-transmembrane domain receptors that bind to extracellular signaling molecules like hormones, neurotransmitters, or chemokines. Upon activation, they initiate a cascade of intracellular signals through G proteins and secondary messengers.
2. Receptor tyrosine kinases (RTKs): These are transmembrane receptors that bind to growth factors, cytokines, or hormones. Activation of RTKs leads to autophosphorylation of specific tyrosine residues, creating binding sites for intracellular signaling proteins such as adapter proteins, phosphatases, and enzymes like Ras, PI3K, and Src family kinases.
3. Second messenger systems: Intracellular second messengers are small molecules that amplify and propagate signals within the cell. Examples include cyclic adenosine monophosphate (cAMP), cyclic guanosine monophosphate (cGMP), diacylglycerol (DAG), inositol triphosphate (IP3), calcium ions (Ca2+), and nitric oxide (NO). These second messengers activate or inhibit various downstream effectors, leading to changes in cellular responses.
4. Signal transduction cascades: Intracellular signaling proteins often form complex networks of interacting molecules that relay signals from the plasma membrane to the nucleus. These cascades involve kinases (protein kinases A, B, C, etc.), phosphatases, and adapter proteins, which ultimately regulate gene expression, cell cycle progression, metabolism, and other cellular processes.
5. Ubiquitination and proteasome degradation: Intracellular signaling pathways can also control protein stability by modulating ubiquitin-proteasome degradation. E3 ubiquitin ligases recognize specific substrates and conjugate them with ubiquitin molecules, targeting them for proteasomal degradation. This process regulates the abundance of key signaling proteins and contributes to signal termination or amplification.

In summary, intracellular signaling pathways involve a complex network of interacting proteins that relay signals from the plasma membrane to various cellular compartments, ultimately regulating gene expression, metabolism, and other cellular processes. Dysregulation of these pathways can contribute to disease development and progression, making them attractive targets for therapeutic intervention.

Epithelial cells are types of cells that cover the outer surfaces of the body, line the inner surfaces of organs and glands, and form the lining of blood vessels and body cavities. They provide a protective barrier against the external environment, regulate the movement of materials between the internal and external environments, and are involved in the sense of touch, temperature, and pain. Epithelial cells can be squamous (flat and thin), cuboidal (square-shaped and of equal height), or columnar (tall and narrow) in shape and are classified based on their location and function.

Cadherins are a type of cell adhesion molecule that play a crucial role in the development and maintenance of intercellular junctions. They are transmembrane proteins that mediate calcium-dependent homophilic binding between adjacent cells, meaning that they bind to identical cadherin molecules on neighboring cells.

There are several types of cadherins, including classical cadherins, desmosomal cadherins, and protocadherins, each with distinct functions and localization in tissues. Classical cadherins, also known as type I cadherins, are the most well-studied and are essential for the formation of adherens junctions, which help to maintain cell-to-cell contact and tissue architecture.

Desmosomal cadherins, on the other hand, are critical for the formation and maintenance of desmosomes, which are specialized intercellular junctions that provide mechanical strength and stability to tissues. Protocadherins are a diverse family of cadherin-related proteins that have been implicated in various developmental processes, including neuronal connectivity and tissue patterning.

Mutations in cadherin genes have been associated with several human diseases, including cancer, neurological disorders, and heart defects. Therefore, understanding the structure, function, and regulation of cadherins is essential for elucidating their roles in health and disease.

'Cercopithecus aethiops' is the scientific name for the monkey species more commonly known as the green monkey. It belongs to the family Cercopithecidae and is native to western Africa. The green monkey is omnivorous, with a diet that includes fruits, nuts, seeds, insects, and small vertebrates. They are known for their distinctive greenish-brown fur and long tail. Green monkeys are also important animal models in biomedical research due to their susceptibility to certain diseases, such as SIV (simian immunodeficiency virus), which is closely related to HIV.

Gene expression profiling is a laboratory technique used to measure the activity (expression) of thousands of genes at once. This technique allows researchers and clinicians to identify which genes are turned on or off in a particular cell, tissue, or organism under specific conditions, such as during health, disease, development, or in response to various treatments.

The process typically involves isolating RNA from the cells or tissues of interest, converting it into complementary DNA (cDNA), and then using microarray or high-throughput sequencing technologies to determine which genes are expressed and at what levels. The resulting data can be used to identify patterns of gene expression that are associated with specific biological states or processes, providing valuable insights into the underlying molecular mechanisms of diseases and potential targets for therapeutic intervention.

In recent years, gene expression profiling has become an essential tool in various fields, including cancer research, drug discovery, and personalized medicine, where it is used to identify biomarkers of disease, predict patient outcomes, and guide treatment decisions.

"Newborn animals" refers to the very young offspring of animals that have recently been born. In medical terminology, newborns are often referred to as "neonates," and they are classified as such from birth until about 28 days of age. During this time period, newborn animals are particularly vulnerable and require close monitoring and care to ensure their survival and healthy development.

The specific needs of newborn animals can vary widely depending on the species, but generally, they require warmth, nutrition, hydration, and protection from harm. In many cases, newborns are unable to regulate their own body temperature or feed themselves, so they rely heavily on their mothers for care and support.

In medical settings, newborn animals may be examined and treated by veterinarians to ensure that they are healthy and receiving the care they need. This can include providing medical interventions such as feeding tubes, antibiotics, or other treatments as needed to address any health issues that arise. Overall, the care and support of newborn animals is an important aspect of animal medicine and conservation efforts.

Transcription factors are proteins that play a crucial role in regulating gene expression by controlling the transcription of DNA to messenger RNA (mRNA). They function by binding to specific DNA sequences, known as response elements, located in the promoter region or enhancer regions of target genes. This binding can either activate or repress the initiation of transcription, depending on the properties and interactions of the particular transcription factor. Transcription factors often act as part of a complex network of regulatory proteins that determine the precise spatiotemporal patterns of gene expression during development, differentiation, and homeostasis in an organism.

A phenotype is the physical or biochemical expression of an organism's genes, or the observable traits and characteristics resulting from the interaction of its genetic constitution (genotype) with environmental factors. These characteristics can include appearance, development, behavior, and resistance to disease, among others. Phenotypes can vary widely, even among individuals with identical genotypes, due to differences in environmental influences, gene expression, and genetic interactions.

Pathologic neovascularization is the abnormal growth of new blood vessels in previously avascular tissue or excessive growth within existing vasculature, which occurs as a result of hypoxia, inflammation, or angiogenic stimuli. These newly formed vessels are often disorganized, fragile, and lack proper vessel hierarchy, leading to impaired blood flow and increased vascular permeability. Pathologic neovascularization can be observed in various diseases such as cancer, diabetic retinopathy, age-related macular degeneration, and chronic inflammation. This process contributes to disease progression by promoting tumor growth, metastasis, and edema formation, ultimately leading to tissue damage and organ dysfunction.

  • EphA5, also known as Ehk1, Bsk, Cek7, Hek7, and Rek7 (1), is a member of the Eph receptor family which binds members of the ephrin ligand family. (rndsystems.com)
  • Ephrin ligands and their receptors, the Eph receptor (Eph) tyrosine kinases, are cell surface molecules that mediate commu-nication between cells. (123dok.org)
  • Catalytic domain of the Protein Tyrosine Kinase, Ephrin Receptor A2. (umbc.edu)
  • This gene belongs to the ephrin receptor subfamily of the protein-tyrosine kinase family. (creativebiomart.net)
  • Ephrin receptor A2 (EphA2) plays dual functions in tumorigenesis through ligand-independent tumor promotion or ligand-dependent tumor suppression. (bvsalud.org)
  • Merrimack has announced positive data from preclinical studies evaluating MM-310, an antibody directed nanotherapeutic (ADN) that encapsulates a newly engineered form of the highly potent chemotherapy docetaxel as a prodrug in an ephrin receptor A2 (EphA2)-targeted liposome. (drugtargetreview.com)
  • Finally, we have studied the role of nanoarchitecture of ephrin ligands in Eph receptor activation. (5dok.org)
  • Over-expression of endogenous fly Eph and RNAi-mediated knock-down of Eph and its ligand ephrin affected sleep architecture and neurophysiology. (sdbonline.org)
  • Binding of the ephrin ligand to EphR requires cell-cell contact since both are anchored to the plasma membrane. (umbc.edu)
  • Eph binds to respective ephrin ligand, through the ligand binding domain and forms a tetrameric complex to activate the kinase domain. (genominfo.org)
  • Unified nomenclature for Eph family receptors and their ligands, the ephrins. (wikipedia.org)
  • In general, class EphA receptors bind GPI-anchored ephrin-A ligands. (umbc.edu)
  • There are ten vertebrate EphA receptors (EphA1-10), which display promiscuous interactions with six ephrin-A ligands. (umbc.edu)
  • The ephrin receptors are divided into 2 groups based on the similarity of their extracellular domain sequences and their affinities for binding ephrin-A and ephrin-B ligands. (creativebiomart.net)
  • This gene encodes a protein that binds ephrin-A ligands. (creativebiomart.net)
  • Ephrin-A2 is a protein that in humans is encoded by the EFNA2 gene. (wikipedia.org)
  • Recent studies in the hippocampus and cerebral cortex show that Eph receptors and ephrins are important in the regulation of synaptic morphology and plasticity. (123dok.org)
  • Therefore, considering the importance of Eph-ephrin class of protein in tumorigenesis, 7,620 clinically reported missense mutations belonging to the class of variables of unknown significance were retrieved from cBioPortal and evaluated for pathogenicity. (genominfo.org)
  • EphRs contain an ephrin binding domain and two fibronectin repeats extracellularly, a transmembrane segment, and a cytoplasmic tyr kinase domain. (umbc.edu)
  • A trans-interaction of Eph-ephrin followed by heterotetramer formation activates the signaling cascade and transforms the kinase domain from closed to open conformation which in-turn, expose the ATP binding pocket [ 5 ]. (genominfo.org)
  • Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. (wikipedia.org)
  • The overall domain organization of EphAs and EphBs are similar, however, ephrin A is GPI anchored to the membrane, whereas ephrin B has an intracellular PDZ binding domain. (genominfo.org)
  • Eph and ephrin are membrane-bound and thus regulate cell-cell interaction, migration, partitioning, and cell adhesion [ 3 ]. (genominfo.org)
  • This withdrawal seems to be distinct from the immediate repulsive effect of ephrin-A2 (ELF-1) and ephrin-A5 (RAGS) seen in the stripe assay because (1) the withdrawal-inducing factor was diffusible, whereas ephrin-A2 and -A5 are membrane-bound, and (2) the withdrawal-inducing factor appeared later in development than ephrin-A2 and -A5. (mpg.de)
  • Eph-ephrin regulates many downstream pathways that lead to physiological events such as cell migration, proliferation, and growth. (genominfo.org)
  • The extracellular domain facilitates binding to ephrin. (genominfo.org)
  • For example, in EphB1/ EphB2/EphB3-deficient mice dendritic spines (the small protru-sions bearing postsynaptic structures) have reduced density and size [3,7,8] while activation of EphB receptors by ephrins induces rapid dendritic spine formation [7,9]. (123dok.org)
  • Based on sequence homology, Eph and ephrin have been classified into EphA/EphrinA and EphB/EphrinB class of families [ 2 ]. (genominfo.org)
  • During embryonic development, ephrin-A4 is expressed in the HIPPOCAMPUS and CEREBRAL CORTEX . (nih.gov)
  • Eph-ephrin as a family is ubiquitously expressed in different tissues [ 4 ]. (genominfo.org)
  • Eph over-expression led to stronger circadian morning anticipation while ephrin knock-down impaired memory. (sdbonline.org)
  • Ephrin/EphR interaction mainly results in cell-cell repulsion or adhesion, making it important in neural development and plasticity, cell morphogenesis, cell-fate determination, embryonic development, tissue patterning, and angiogenesis. (umbc.edu)
  • Utilising fly genetics, this study generated the first Drosophila model of human wild-type and P460L mutant EphA1 and tested the effects of Eph /ephrin signalling on AD-relevant behaviour and neurophysiology. (sdbonline.org)
  • An ephrin that was originally identified as the product of an early response gene induced by TUMOR NECROSIS FACTORS. (umassmed.edu)
  • The resulting downstream signals occur bidirectionally in both EphR-expressing cells (forward signaling) and ephrin-expressing cells (reverse signaling). (umbc.edu)
  • The Eph-ephrin complex follows an exclusive signaling pattern wherein either Eph activates Ephrin for reverse signaling, or Ephrin activates Eph for forward signaling [ 4 ]. (genominfo.org)
  • The Eph/ephrin families also appear to play a role in angiogenesis (3). (rndsystems.com)
  • These results demonstrate a role of Eph/ephrin signalling in a range of behaviours affected in AD. (sdbonline.org)
  • Ephrins and Eph receptors are especially highly expressed in the embryonic nervous system, where their signalling is important for proper axonal pathfinding and to establish topographic projections [1-3]. (123dok.org)
  • To understand the mechanisms through which EBV infects epithelial cells, we integrated microarray and RNA interference screen analyses and found that Ephrin receptor A2 (EphA2) is important for EBV entry into the epithelial cells. (houstonmethodist.org)
  • The EphA2 Ephrin-binding domain and fibronectin type III repeats domain were essential for EphA2-mediated EBV infection, while the intracellular domain was dispensable. (houstonmethodist.org)
  • The erythropoietin-producing hepatoma A2 receptor (EphA2) is a tyrosine kinase overexpressed by tumor stroma and cancer cells. (nih.gov)
  • 2. The clinical significance of EphA2 and Ephrin A-1 in epithelial ovarian carcinomas. (nih.gov)
  • 9. C1GALT1 is associated with poor survival and promotes soluble Ephrin A1-mediated cell migration through activation of EPHA2 in gastric cancer. (nih.gov)
  • 17. The ephrin-A1 ligand and its receptor, EphA2, are expressed during tumor neovascularization. (nih.gov)
  • 19. Higher expression of EphA2 and ephrin-A1 is related to favorable clinicopathological features in pathological stage I non-small cell lung carcinoma. (nih.gov)
  • On epithelial cells the receptors for EBV have been identified as the ephrin receptor A2 (EphA2) and intergrins avb5, avb6, and avb8. (fredhutch.org)
  • EphA4 activation leads autophosphorylation of Tyr-596 and Tyr-602, and the conserved sites in EphA2 are required for binding to the GEFs, Vav2 and Vav3, and ephrin-induced cell migration. (ecmbio.com)
  • Unified nomenclature for Eph family receptors and their ligands, the ephrins. (wikipedia.org)
  • 6. Expression of Eph receptors and their ligands, ephrins, during lipopolysaccharide fever in rats. (nih.gov)
  • Ephrin-B1, also known as LERK-2, ELK-L, EFL-3, Cek5-L, and STRA-1 (1), is a member of the ephrin ligand family which binds members of the Eph receptor family. (rndsystems.com)
  • EphA7, also known as Mdk1, Hek11, Ehk3, Ebk, and Cek11 (1), is a member of the Eph receptor family which binds members of the ephrin ligand family. (rndsystems.com)
  • Ephrin-A2 also known as EFNA2 or EPH-related receptor tyrosine kinase ligand 6, is a member of the ephrin family. (betalifesci.com)
  • Based on their structures and sequence relationships, ephrins are divided into the ephrin-A (EFNA) class, which are anchored to the membrane by a glycosylphosphatidylinositol linkage, and the ephrin-B (EFNB) class, which are transmembrane proteins. (wikipedia.org)
  • Measured by its ability to compete with Biotinylated Recombinant Human Ephrin‑A5 Fc Chimera (Catalog # BT374 ) for binding to immobilized recombinant mouse Eph-A3 Fc Chimera in a functional ELISA assay. (novusbio.com)
  • The extracellular domains of human and mouse Ephrin-B1 share 94% amino acid identity. (rndsystems.com)
  • 13. Human endometrial epithelial cells express ephrin A1: possible interaction between human blastocysts and endometrium via Eph-ephrin system. (nih.gov)
  • 15. Bifunctional role of ephrin A1-Eph system in stimulating cell proliferation and protecting cells from cell death through the attenuation of ER stress and inflammatory responses in bovine mammary epithelial cells. (nih.gov)
  • Eph receptors are classified into 10 EphA and 6 EphB receptors, which preferentially bind to the type A and type B ephrins, respectively. (ecmbio.com)
  • Ephrin‑A5 preferentially interacts with receptors in the EphA family but also with EphB2 (3). (novusbio.com)
  • Ephrin-A2 regulates the position-specific affinity of limb mesenchyme and is involved in cartilage pattern formation in the limb. (betalifesci.com)
  • 4. Eph-ephrin A system regulates human choriocarcinoma-derived JEG-3 cell invasion. (nih.gov)
  • Eph/ephrin interactions are implicated in axon guidance, neural crest cell migration, establishment of segmental boundaries, and formation of angiogenic capillary plexi. (betalifesci.com)
  • It interacts in cis with EphA3 on retinal axon growth cones which reduces axonal sensitivity to Ephrin‑A5 in trans (13). (novusbio.com)
  • Eph‑Ephrin interactions are widely involved in the regulation of cell migration, tissue morphogenesis, and cancer progression (1, 2). (novusbio.com)
  • 7. Roles of EphA1/A2 and ephrin-A1 in cancer. (nih.gov)
  • Ephrin‑A5 repels migrating axons by inducing growth cone collapse and neurite retraction and by inhibiting the neurotrophic effects of NGF and BDNF (3, 11, 12). (novusbio.com)
  • Rac1 mediated endocytosis during ephrin-A2 and Semaphorin 3A induced growth cone collapse. (umn.edu)
  • This is evidence of species specific ephrin receptor usage by a henipavirus, and implicates additional ephrin receptors in potential zoonotic transmission. (rcsb.org)
  • Structural and functional analyses reveal promiscuous and species specific use of ephrin receptors by Cedar virus. (anl.gov)
  • The CedV G receptor-binding site is structurally distinct from other henipaviruses, underlying its capability to accommodate additional ephrin receptors. (rcsb.org)
  • This gene encodes a member of the ephrin family. (wikipedia.org)
  • Ephrin-A2 and their Eph family of receptor tyrosine kinases are expressed by cells of the SVZ. (betalifesci.com)
  • Description: This is Double-antibody Sandwich Enzyme-linked immunosorbent assay for detection of Human Aldehyde Dehydrogenase 1 Family, Member A2 (ALDH1A2) in serum, plasma, tissue homogenates and other biological fluids. (lipidx.org)
  • Description: A sandwich ELISA kit for detection of Aldehyde Dehydrogenase 1 Family, Member A2 from Human in samples from blood, serum, plasma, cell culture fluid and other biological fluids. (lipidx.org)
  • PVDF membrane was probed with 1 µg/mL of Rat Anti-Mouse Ephrin-B1 Monoclonal Antibody (Catalog # MAB4731) followed by HRP-conjugated Anti-Rat IgG Secondary Antibody (Catalog # HAF005 ). (rndsystems.com)
  • A GLYCOINOSITOL PHOSPHOLIPID MEMBRANE ANCHOR -containing ephrin with a high affinity for the EPHA3 RECEPTOR. (bvsalud.org)
  • Detects mouse Ephrin-B1 in direct ELISAs and Western blots. (rndsystems.com)
  • Detection of Mouse Ephrin‑B1 by Western Blot. (rndsystems.com)
  • A specific band was detected for Ephrin-B1 at approximately 45 kDa (as indicated). (rndsystems.com)
  • 14. Mapping the Universe of Eph Receptor and Ephrin Ligand Transcripts in Epithelial and Fiber Cells of the Eye Lens. (nih.gov)
  • We demonstrate that CedV also enters cells through additional B- and A-class ephrins (ephrin-B1, ephrin-A2, and ephrin-A5) and report the crystal structure of the CedV G ectodomain alone and in complex with ephrin-B1 or ephrin-B2. (rcsb.org)
  • We demonstrate that CedV also enters cells through additional B- and A-class ephrins (ephrin-B1, ephrin-A2, and ephrin-A5) and report the crystal This web page summarizes information in PubChem about patent US-8324283-B2. (netlify.app)
  • Ephrin‑A5 is expressed in multiple tissues during development, particularly in the brain (5, 6). (novusbio.com)

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